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Structural Research of Monomeric/Dimeric Beta-Barrel Membrane Proteins

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Beta-barrel membrane proteins are a class of proteins that are embedded in the lipid bilayer of the cell membrane and play a vital role in the transport of various molecules across the membrane. These proteins consist of multiple β-strands that form a cylindrical shape with a central pore and can exist as monomers or form dimers or higher-order oligomers in the membrane.

Recent advances in structural biology techniques have enabled the determination of the high-resolution structures of several beta-barrel membrane proteins in their monomeric and dimeric forms. For example, the dynamic NMR structures of AlkL, a protein that plays a role in transporting hydrophobic molecules across the membrane, revealed a β-barrel structure with hydrophobic residues lining the inside of the barrel. The crystal structure of OmpF, a protein that forms a dimeric structure in the membrane, showed that the dimerization is mediated by hydrogen bonds and van der Waals interactions between the β-strands.

MR  structure and dynamics of AlkL.Figure 1. NMR structure and dynamics of AlkL. (Schubeis T, et al., 2020)

ProteinOrganismMethodResolutionPDB Entry ID
TolC outer membrane protein (expressed in E. coli)Escherichia coliX-ray diffraction2.10 Å1EK9
TolC outer membrane protein, ligand blockedEscherichia coliX-ray diffraction2.75 Å1TQQ
TolC outer membrane protein (Y362F, R367E), partially open state (expressed in E. coli)Escherichia coliX-ray diffraction3.20 Å2VDE
TolC outer membrane protein in a nanodisc with colicin E1 fragment (expressed in E. coli)Escherichia coliCryo-EM single particle analysis3.09 Å6WXH
TolC outer membrane protein in complex with KlebC (expressed in E. coli)Klebsiella quasipneumoniaeCryo-EM single particle analysis3.20 Å7NG8
CmeC bacterial multi-drug efflux transporter outer membrane channel (expressed in E. coli)Campylobacter jejuniX-ray diffraction2.37 Å4MT4
VceC outer membrane protein (expressed in E. coli)Vibrio choleraeX-ray diffraction1.80 Å1YC9
OprM drug discharge outer membrane protein (expressed in Pseudomonas aeruginosa)Pseudomonas aeruginosaX-ray diffraction2.56 Å1WP1
OprM drug discharge outer membrane protein (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.40 Å3D5K
OprN drug discharge outer membrane protein, I4 space group (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.70 Å5AZO
OprJ drug discharge outer membrane protein (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction3.10 Å5AZS
ST50 discharge outer membrane protein (expressed in E. coli)Salmonella entericaX-ray diffraction2.98 Å5BUN
CusC heavy metal discharge outer membrane proteinEscherichia coliX-ray diffraction2.30 Å3PIK
CusC heavy metal discharge outer membrane protein (expressed in E. coli)Escherichia coliX-ray diffraction2.09 Å4K7R
apo BtuB cobalamin transporter (expressed in E. coli)Escherichia coliX-ray diffraction2.00 Å1NQE
BtuB with bound colicin E3 R-domain (expressed in E. coli)Escherichia coliX-ray diffraction2.75 Å1UJW
apo BtuB by in meso crystallization (expressed in E. coli)Escherichia coliX-ray diffraction1.95 Å2GUF
BtuB in complex with TonB (expressed in E. coli)Escherichia coliX-ray diffraction2.10 Å2GSK
BtuB with bound colicin E2 R-domain (expressed in E. coli)Escherichia coliX-ray diffraction3.50 Å2YSU
apo BtuB V10R1 spin-labeled (expressed in E. coli)Escherichia coliX-ray diffraction2.44 Å3M8B
Colicin I receptor Cir in complex with Colicin Ia binding domain (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å2HDI
OmpA (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å1BXW
OmpA (expressed in E. coli)Escherichia coliX-ray diffraction1.65 Å1QJP
OmpA (expressed in E. coli)Escherichia coliSolution NMR/1G90
OmpA (expressed in E. coli)Escherichia coliSolution NMR/2GE4
OmpA with four shortened loops (expressed in E. coli)Escherichia coliSolution NMR/2JMM
OmpA (expressed in E. coli)Klebsiella pneumoniaeSolution NMR/2K0L
OmpT outer membrane protease (expressed in E. coli)Escherichia coliX-ray diffraction2.60 Å1I78
Pla Plasminogen activator (native 1) (expressed in E. coli)Yersinia pestisX-ray diffraction1.85 Å2X55
OmpW outer membrane protein (expressed in E. coli)Escherichia coliX-ray diffraction2.70 Å2F1V
OmpW outer membrane protein (expressed in E. coli)Escherichia coliSolution NMR/2MHL
AlkL passive importer of hydrophobic molecules in DMPC lipid bilayer (expressed in E. coli)Pseudomonas oleovoransSolid-state NMR/6QWR
CarO outer membrane protein, isoform 1 (expressed in E. coli)Acinetobacter baumanniiX-ray diffraction2.70 Å4RL9
OprF outer membrane protein, N-terminal β-barrel domain (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction1.60 Å4RLC
OprG outer membrane protein (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.40 Å2X27
OprH, outer membrane protein H (expressed in E. coli)Pseudomonas aeruginosaSolution NMR/2LHF
OmpX (expressed in E. coli)Escherichia coliX-ray diffraction1.90 Å1QJ8
OmpX (expressed in E. coli)Escherichia coliSolution NMR/1ORM
OmpX (expressed in E. coli)Escherichia coliSolution NMR/1Q9F
OmpX in optimized nanodiscs (expressed in E. coli)Escherichia coliSolution NMR/2M06
Ail adhesion protein (expressed in E. coli)Yersinia pestisX-ray diffraction1.80 Å3QRA
Ail adhesion protein, decylphosphocholine micelles (expressed in E. coli)Yersinia pestisSolution NMR/2N2M
Ail adhesion protein (expressed in E. coli)Yersinia pestisSolution NMR/5VJ8
TtoA Outer Membrane Protein (OMP) (expressed in Thermus thermophilus)Thermus thermophilusX-ray diffraction2.80 Å3DZM
OmpLA (PldA) outer membrane phospholipase A monomer (expressed in E. coli)Escherichia coliX-ray diffraction2.17 Å1QD5
OmpLA (PldA) outer membrane phospholipase A monomer with Ca++ (expressed in E. coli)Escherichia coliX-ray diffraction2.60 Å1FW2
OmpLA (PldA) active-site mutant (N156A), pH 6.1 (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å1ILZ
OpcA adhesin proteinNeisseria meningitidisX-ray diffraction2.03 Å1K24
OpcA adhesin protein (expressed in E. coli)Neisseria meningitidisX-ray diffraction1.95 Å2VDF
NspA surface protein (expressed in E. coli)Neisseria meningitidisX-ray diffraction2.55 Å1P4T
NanC Porin, model for KdgM porin family (expressed in E. coli)Escherichia coliX-ray diffraction1.80 Å2WJR
PagL LPS 3-O-deacylase (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.00 Å2ERV
LpxR lipid A deacylase (expressed in E. coli)Salmonella entericaX-ray diffraction1.90 Å3FID
PagP outer membrane palimitoyl transferease (expressed in E. coli)Escherichia coliSolution NMR/1MM4
PagP outer membrane palimitoyl transferease (expressed in E. coli)Escherichia coliX-ray diffraction1.90 Å1THQ
PagP outer membrane palimitoyl transferease crystallized from SDS/Co-solvent (expressed in E. coli)Escherichia coliX-ray diffraction1.40 Å3GP6
FadL long-chain fatty acid transporter (expressed in E. coli)Escherichia coliX-ray diffraction2.60 Å1T16
FadL long-chain fatty acid transporter A77E/S100R mutant (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å3DWN
FadL long-chain fatty acid transporter D348R mutant (expressed in E. coli)Escherichia coliX-ray diffraction2.60 Å3PGR
FadL homologue long-chain fatty acid transporter (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.20 Å3DWO
YebT lipid transporter, domains 1-4 (expressed in E. coli)Escherichia coliCryo-EM single particle analysis3.10 Å6KZ3
FauA alcaligin outer membrane transporter (expressed in E. coli)Bordetella pertussisX-ray diffraction2.33 Å3EFM
TodX hydrocarbon transporter (expressed in E. coli)Pseudomonas putidaX-ray diffraction2.60 Å3BS0
TbuX hydrocarbon transporter (expressed in E. coli)Ralstonia pickettiiX-ray diffraction3.20 Å3BRY
Tsx nucleoside transporter (apoprotein) (expressed in E. coli)Escherichia coliX-ray diffraction3.01 Å1TLY
FhuA, Ferrichrome-iron receptor without ligandEscherichia coliX-ray diffraction2.74 Å1BY3
FhuA (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å2FCP
FhuA-AW140-LPS (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å1QFG
FhuA in complex with albomycin (expressed in E. coli)Escherichia coliX-ray diffraction3.10 Å1QKC
FhuA in complex with lipopolysaccharide and rifamycin CGP4832 (expressed in E. coli)Escherichia coliX-ray diffraction2.90 Å1FI1
FhuA in complex withTonB (expressed in E. coli)Escherichia coliX-ray diffraction3.30 Å2GRX
FhuA in complex with lasso peptide microcin J25 (MccJ25) (expressed in E. coli)Escherichia coliX-ray diffraction2.30 Å4CU4
FhuA in complex with the superinfection exclusion lipoprotein Llp (expressed in E. coli)Escherichia coliX-ray diffraction3.37 Å8A60
FyuA siderophore transporter (expressed in E. coli)Yersinia pestisX-ray diffraction3.20 Å4EPA
FepA, Ferric enterobactin receptorEscherichia coliX-ray diffraction2.40 Å1FEP
Fiu Ferric-Catecholate import receptor, open C222(1) crystal form (expressed in E. coli)Escherichia coliX-ray diffraction2.10 Å6BPN
FecA, siderophore transporter (expressed in E. coli)Escherichia coliX-ray diffraction2.00 Å1KMO
FecA, siderophore transporter (no ligand) (expressed in E. coli)Escherichia coliX-ray diffraction2.50 Å1PNZ
FecA, siderophore transporter periplasmic signalling domain (expressed in E. coli)Escherichia coliSolution NMR/2D1U
PiuA siderophore receptor (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction1.90 Å5FOK
PiuD siderophore receptor (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.30 Å5NEC
PiuA siderophore receptor (expressed in E. coli)Acinetobacter baumanniiX-ray diffraction1.94 Å5FP1
PirA siderophore receptor (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.97 Å5FP2
PirA siderophore receptor (expressed in E. coli)Acinetobacter baumanniiX-ray diffraction2.83 Å5FR8
HasR heme-uptake receptor in complex with HasA hemophore and heme (expressed in E. coli)Serratia marcescensX-ray diffraction2.70 Å3CSL
ShuA heme-uptake receptor in complex with HasA hemophore and heme (expressed in E. coli)Shigella dysenteriaeX-ray diffraction2.60 Å3FHH
FptA pyochelin siderophore transporterPseudomonas aeruginosaX-ray diffraction2.00 Å1XKW
FptA pyochelin siderophore transporter (expressed in Pseudomonas fluorescens)Pseudomonas fluorescensX-ray diffraction3.26 Å3QLB
FpvA, Pyoverdine receptor (expressed in Pseudomonas aeruginosa)Pseudomonas aeruginosaX-ray diffraction3.60 Å1XKH
FpvA, Pyoverdine receptor (apo form) (expressed in Pseudomonas aeruginosa)Pseudomonas aeruginosaX-ray diffraction2.77 Å2O5P
FpvA, Full-length structure bound to iron-pyoverdine (expressed in Pseudomonas aeruginosa)Pseudomonas aeruginosaX-ray diffraction2.73 Å2IAH
AlgE alginate export protein (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.30 Å3RBH
AlgE alginate export protein (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction1.90 Å4AFK
AlgE alginate export protein at 100 K (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.90 Å4XNL
AlgK–AlgX alginate export protein complex (expressed in E. coli)Pseudomonas putidaX-ray diffraction2.46 Å7ULA
P pilus usher translocation domain, PapC130-640 (expressed in E. coli)Escherichia coliX-ray diffraction3.20 Å2VQI
P pilus usher translocation domain, PapC146-637 (expressed in E. coli)Escherichia coliX-ray diffraction3.15 Å3FIP
P pilus FimD usher bound to FimC:FimH substrate (expressed in E. coli)Escherichia coliX-ray diffraction2.80 Å3RFZ
P pilus FimD usher in complex with FimC:FimF:FimG:FimH (expressed in E. coli)Escherichia coliX-ray diffraction3.80 Å4J3O
P pilus assembly intermediate (FimD-FimC-FimF-FimG-FimH), conformer 1 (expressed in E. coli)Escherichia coliCryo-EM single particle analysis4.00 Å6E14
P pilus tip assembly intermediate PapC-PapD-PapK-PapF-PapG (expressed in E. coli)Escherichia coliCryo-EM single particle analysis7.60 Å7LHI
Transferrin binding protein A (TbpA) in complex with human transferrin (expressed in E. coli)Neisseria meningitidisX-ray diffraction2.60 Å3V8X
Wzi outer-membrane lectinEscherichia coliX-ray diffraction2.64 Å2YNK
Opa60 for receptor-mediated engulfment, EXPLOR refined (expressed in Neisseria gonorrhoeae)Neisseria gonorrhoeaeSolution NMR/2MLH
CsgG bacterial amyloid secretion channel (expressed in E. coli)Escherichia coliX-ray diffraction3.59 Å4UV3
CsgG bacterial amyloid secretion channel (expressed in E. coli)Escherichia coliX-ray diffraction3.10 Å4Q79
CsgG-CsgF complex involved in curli biogenesis (expressed in E. coli)Escherichia coliCryo-EM single particle analysis2.94 Å6LQH
CsgG-CsgF complex involved in curli biogenesis (expressed in E. coli)Escherichia coliCryo-EM single particle analysis3.38 Å6L7A
CsgG-CsgF complex involved in curli biogenesis (expressed in E. coli)Escherichia coliCryo-EM single particle analysis3.40 Å6SI7
FusA plant-ferredoxin receptor (expressed in E. coli)Pectobacterium atrosepticumCryo-EM single particle analysis3.20 Å4ZGV
Omp33 outer membrane protein (expressed in E. coli)Acinetobacter baumanniiX-ray diffraction2.10 Å6GIE
FrpB TonB-dependent iron transporter (expressed in E. coli)Neisseria meningitidisX-ray diffraction2.40 Å4AIP
FhuE TonB-dependent transporter (expressed in E. coli)Escherichia coliX-ray diffraction2.00 Å6E4V
YncD TonB-dependent transporter (expressed in E. coli)Escherichia coliX-ray diffraction2.96 Å6V81
PfeA ferric enterobactin receptor, apo form (expressed in E. coli)Pectobacterium atrosepticumX-ray diffraction2.12 Å5M9B
PfeA ferric enterobactin receptor in complex with TCV (expressed in E. coli)Pseudomonas aeruginosaX-ray diffraction2.57 Å5NC3
BcsC cellulose synthase outer membrane channel (expressed in E. coli)Escherichia coliX-ray diffraction1.85 Å6TZK
ZnuD zinc transporter (expressed in E. coli)Neisseria meningitidisX-ray diffraction3.20 Å4RDT
MtrE Outer Membrane Channel (expressed in E. coli)Neisseria gonorrhoeaeX-ray diffraction3.29 Å4MT0
LetB lipophilic Envelope-spanning Tunnel B, model 1 (expressed in E. coli)Escherichia coliCryo-EM single particle analysis3.46 Å6V0C
PcoB copper transporter (expressed in E. coli)Escherichia coliX-ray diffraction2.00 Å7PGE

Table 1. Structural Research of Beta-Barrel Membrane Proteins: Monomeric/Dimeric.

Creative Biostructure is a reliable provider of structural biology services that enable the determination of the high-resolution structures of beta-barrel membrane proteins. Our team of expert scientists utilizes state-of-the-art techniques such as X-ray crystallography, cryo-electron microscopy, and nuclear magnetic resonance spectroscopy to provide clients with accurate structural data. We offer a comprehensive range of services that include protein expression and purification, crystallization, structure determination, and analysis. In addition, our team of experienced scientists can perform high-quality NMR experiments to provide information on protein dynamics and interactions with ligands or other proteins.

If you are interested in leveraging the power of structural biology to explore the monomeric and dimeric structure of beta-barrel membrane proteins, please contact us today. Our custom-designed solutions are tailored to meet the unique requirements of each client and are backed by our commitment to quality and customer satisfaction.

References

  1. Budiardjo S J, et al. Colicin E1 opens its hinge to plug TolC. Elife. 2022, 11: e73297.
  2. Schubeis T, et al. A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL. Proceedings of the National Academy of Sciences. 2020, 117(35): 21014-21021.
  3. Isom G L, et al. LetB structure reveals a tunnel for lipid transport across the bacterial envelope. Cell. 2020, 181(3): 653-664. e19.

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