5Z8O
Structural of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis
Summary for 5Z8O
Entry DOI | 10.2210/pdb5z8o/pdb |
Descriptor | Cyclase/dehydrase (2 entities in total) |
Functional Keywords | msmeg_0129, start domain, mycobacterium smegmatis, unknown function |
Biological source | Mycobacterium smegmatis str. MC2 155 |
Total number of polymer chains | 2 |
Total formula weight | 32683.01 |
Authors | |
Primary citation | Zheng, S.,Zhou, Y.,Fleming, J.,Zhou, Y.,Zhang, M.,Li, S.,Li, H.,Sun, B.,Liu, W.,Bi, L. Structural and genetic analysis of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis. FEBS Lett., 592:1445-1457, 2018 Cited by PubMed Abstract: Mycobacterium tuberculosis is a notorious pathogen that continues to threaten human health. Rv0164, an antigen of both T- and B cells conserved across mycobacteria, and MSMEG_0129, its close homolog in Mycobacterium smegmatis, are predicted members of the START domain superfamily, but their molecular function is unknown. Here, gene knockout studies demonstrate MSMEG_0129 is essential for bacterial growth, suggesting Rv0164 may be a potential drug target. The MSMEG_0129 crystal structure determined at 1.95 Å reveals a fold similar to that in polyketide aromatase/cyclases ZhuI and TcmN from Streptomyces sp. Structural comparisons and docking simulations, however, infer that MSMEG_0129 and Rv0164 are unlikely to catalyze polyketide aromatization/cyclization, but probably play an irreplaceable role during mycobacterial growth, for example, in lipid transfer during cell envelope synthesis. PubMed: 29512898DOI: 10.1002/1873-3468.13024 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report