Structural Research of Bacterial Cell Division Proteins
Bacterial cell division, the process by which one parent cell divides into two identical daughter cells, is a highly regulated process to ensure proper segregation of genetic material. Disturbance of this process could lead to the formation of abnormal cells, which in turn could have serious implications for bacterial survival. Over the years, there has been a significant leap in the understanding of molecular mechanisms that underlie bacterial cell division, with a particular emphasis on structural and functional characterization of critical proteins involved in the process.
In the scope of bacterial cell division, one of the primary proteins is CrgA. CrgA is discovered in Mycobacterium tuberculosis, the bacterium responsible for causing tuberculosis. A recent study utilized X-ray crystallography and NMR spectroscopy to decipher the structure of CrgA embedded in lipid bilayers. Findings from the study showed that CrgA forms a dimeric structure that interacts with lipid bilayers and FtsZ, another protein that plays a critical role in bacterial cell division.
Figure 1. The structure of Mtb CrgA as a platform for assembling other interacting proteins. (Das N, et al., 2015)
Protein | Organism | Method | Resolution | PDB Entry ID |
CrgA, a cell division structural and regulatory protein, in lipid bilayers (expressed in E. coli) | Mycobacterium tuberculosis | Solid-state NMR | / | 2MMU |
Table 1. Structural Research of Bacterial Cell Division Proteins.
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Reference
- Das N, et al. Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers. Proceedings of the National Academy of Sciences. 2015, 112(2): E119-E126.