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7BVH

Crystal structure of arabinosyltransferase EmbC2-AcpM2 complex from Mycobacterium smegmatis complexed with di-arabinose

Summary for 7BVH
Entry DOI10.2210/pdb7bvh/pdb
Related PRD IDPRD_900018
DescriptorIntegral membrane indolylacetylinositol arabinosyltransferase EmbC, Meromycolate extension acyl carrier protein, alpha-D-arabinofuranose-(1-5)-alpha-D-arabinofuranose, ... (7 entities in total)
Functional Keywordscell wall synthesis, arabinosyltransferase, drug target, transferase
Biological sourceMycolicibacterium smegmatis MC2 155
More
Total number of polymer chains4
Total formula weight264975.47
Authors
Zhao, Y.,Zhang, L.,Wu, L.J.,Wang, Q.,Li, J.,Besra, G.S.,Rao, Z.H. (deposition date: 2020-04-10, release date: 2020-04-29, Last modification date: 2020-07-29)
Primary citationZhang, L.,Zhao, Y.,Gao, Y.,Wu, L.,Gao, R.,Zhang, Q.,Wang, Y.,Wu, C.,Wu, F.,Gurcha, S.S.,Veerapen, N.,Batt, S.M.,Zhao, W.,Qin, L.,Yang, X.,Wang, M.,Zhu, Y.,Zhang, B.,Bi, L.,Zhang, X.,Yang, H.,Guddat, L.W.,Xu, W.,Wang, Q.,Li, J.,Besra, G.S.,Rao, Z.
Structures of cell wall arabinosyltransferases with the anti-tuberculosis drug ethambutol.
Science, 368:1211-1219, 2020
Cited by
PubMed Abstract: The arabinosyltransferases EmbA, EmbB, and EmbC are involved in cell wall synthesis and are recognized as targets for the anti-tuberculosis drug ethambutol. In this study, we determined cryo-electron microscopy and x-ray crystal structures of mycobacterial EmbA-EmbB and EmbC-EmbC complexes in the presence of their glycosyl donor and acceptor substrates and with ethambutol. These structures show how the donor and acceptor substrates bind in the active site and how ethambutol inhibits arabinosyltransferases by binding to the same site as both substrates in EmbB and EmbC. Most drug-resistant mutations are located near the ethambutol binding site. Collectively, our work provides a structural basis for understanding the biochemical function and inhibition of arabinosyltransferases and the development of new anti-tuberculosis agents.
PubMed: 32327601
DOI: 10.1126/science.aba9102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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