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<StructureSection load='7nvh' size='340' side='right'caption='[[7nvh]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
<StructureSection load='7nvh' size='340' side='right'caption='[[7nvh]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7nvh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NVH FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NVH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AV0:2-decyl-2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}dodecyl+4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside'>AV0</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.02&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0206c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AV0:2-decyl-2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}dodecyl+4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside'>AV0</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=7nvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nvh OCA], [https://pdbe.org/7nvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nvh RCSB], [https://www.ebi.ac.uk/pdbsum/7nvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nvh ProSAT]</span></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=7nvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nvh OCA], [https://pdbe.org/7nvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nvh RCSB], [https://www.ebi.ac.uk/pdbsum/7nvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nvh ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tuberculosis (TB) is the leading cause of death from a single infectious agent and in 2019 an estimated 10 million people worldwide contracted the disease. Although treatments for TB exist, continual emergence of drug-resistant variants necessitates urgent development of novel antituberculars. An important new target is the lipid transporter MmpL3, which is required for construction of the unique cell envelope that shields Mycobacterium tuberculosis (Mtb) from the immune system. However, a structural understanding of the mutations in Mtb MmpL3 that confer resistance to the many preclinical leads is lacking, hampering efforts to circumvent resistance mechanisms. Here, we present the cryoelectron microscopy structure of Mtb MmpL3 and use it to comprehensively analyze the mutational landscape of drug resistance. Our data provide a rational explanation for resistance variants local to the central drug binding site, and also highlight a potential alternative route to resistance operating within the periplasmic domain.
Cryo-EM structure and resistance landscape of M. tuberculosis MmpL3: An emergent therapeutic target.,Adams O, Deme JC, Parker JL, Fowler PW, Lea SM, Newstead S Structure. 2021 Jun 28. pii: S0969-2126(21)00217-3. doi:, 10.1016/j.str.2021.06.013. PMID:34242558<ref>PMID:34242558</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7nvh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Adams, O]]
[[Category: Adams O]]
[[Category: Deme, J C]]
[[Category: Deme JC]]
[[Category: Lea, S M]]
[[Category: Lea SM]]
[[Category: Newstead, S]]
[[Category: Newstead S]]
[[Category: Parker, J L]]
[[Category: Parker JL]]
[[Category: Membrane protein]]
[[Category: Transporter]]

Latest revision as of 11:58, 14 July 2024

Cryo-EM structure of the mycolic acid transporter MmpL3 from M. tuberculosisCryo-EM structure of the mycolic acid transporter MmpL3 from M. tuberculosis

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.02Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

7nvh, resolution 3.02Å

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