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5Z8O

Structural of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis

Summary for 5Z8O
Entry DOI10.2210/pdb5z8o/pdb
DescriptorCyclase/dehydrase (2 entities in total)
Functional Keywordsmsmeg_0129, start domain, mycobacterium smegmatis, unknown function
Biological sourceMycobacterium smegmatis str. MC2 155
Total number of polymer chains2
Total formula weight32683.01
Authors
Zheng, S.,Liu, W.,Bi, L. (deposition date: 2018-01-31, release date: 2018-03-21, Last modification date: 2023-11-22)
Primary citationZheng, 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: 29512898
DOI: 10.1002/1873-3468.13024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

229380

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