7bvc
From Proteopedia
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<StructureSection load='7bvc' size='340' side='right'caption='[[7bvc]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='7bvc' size='340' side='right'caption='[[7bvc]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BVC FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=95E:Ethambutol'>95E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=F8L:[(2Z,6E,10E,14Z,18E,22Z,26Z)-3,7,11,15,19,23,27,31,35,39-decamethyltetraconta-2,6,10,14,18,22,26,30,34,38-decaenyl]+[(2S,3S,4S,5R)-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]+hydrogen+phosphate'>F8L</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=95E:Ethambutol'>95E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=F8L:[(2Z,6E,10E,14Z,18E,22Z,26Z)-3,7,11,15,19,23,27,31,35,39-decamethyltetraconta-2,6,10,14,18,22,26,30,34,38-decaenyl]+[(2S,3S,4S,5R)-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]+hydrogen+phosphate'>F8L</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7bvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bvc OCA], [https://pdbe.org/7bvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bvc RCSB], [https://www.ebi.ac.uk/pdbsum/7bvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bvc ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
- | == Function == | ||
- | [[http://www.uniprot.org/uniprot/ACPM_MYCS2 ACPM_MYCS2]] Acyl carrier protein involved in meromycolate extension. | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The arabinosyltransferases EmbA, EmbB, and EmbC are involved in Mycobacterium tuberculosis cell wall synthesis and are recognized as the targets for the anti-tuberculosis drug ethambutol. We have 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 by binding to the same site as both substrates in EmbB and EmbC. The majority of drug-resistant mutations are located nearby to the ethambutol-binding site. Collectively, our work provides a structural basis for understanding the biochemical function and inhibition of arabinosyltransferases and development of new anti-tuberculosis agents. | ||
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- | Structures of cell wall arabinosyltransferases with the anti-tuberculosis drug ethambutol.,Zhang L, Zhao Y, Gao Y, Wu L, Gao R, Zhang Q, Wang Y, Wu C, Wu F, Gurcha SS, Veerapen N, Batt SM, Zhao W, Qin L, Yang X, Wang M, Zhu Y, Zhang B, Bi L, Zhang X, Yang H, Guddat LW, Xu W, Wang Q, Li J, Besra GS, Rao Z Science. 2020 Apr 23. pii: science.aba9102. doi: 10.1126/science.aba9102. PMID:32327601<ref>PMID:32327601</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 7bvc" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Indolylacetylinositol arabinosyltransferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Besra GS]] | |
- | + | [[Category: Gao Y]] | |
- | [[Category: Besra | + | [[Category: Li J]] |
- | [[Category: Gao | + | [[Category: Rao Z]] |
- | [[Category: Li | + | [[Category: Wang Q]] |
- | [[Category: Rao | + | [[Category: Zhang L]] |
- | [[Category: Wang | + | [[Category: Zhao Y]] |
- | [[Category: Zhang | + | |
- | [[Category: Zhao | + | |
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Current revision
Cryo-EM structure of Mycobacterium smegmatis arabinosyltransferase EmbA-EmbB-AcpM2 in complex with ethambutol
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Categories: Large Structures | Besra GS | Gao Y | Li J | Rao Z | Wang Q | Zhang L | Zhao Y