7k1v

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<StructureSection load='7k1v' size='340' side='right'caption='[[7k1v]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
<StructureSection load='7k1v' size='340' side='right'caption='[[7k1v]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7k1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K1V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7k1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K1V FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6xly|6xly]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pepO, zmp1, DSI38_14250, E5M52_00710, ERS007679_00756, ERS007681_00890, ERS007688_01723, ERS007720_00395, ERS007722_01585, ERS007741_01200, ERS013471_01326, ERS023446_01760, ERS075361_00622, ERS094182_00084, F6W99_02844, FRD82_01875 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7k1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k1v OCA], [https://pdbe.org/7k1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k1v RCSB], [https://www.ebi.ac.uk/pdbsum/7k1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k1v 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=7k1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k1v OCA], [https://pdbe.org/7k1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k1v RCSB], [https://www.ebi.ac.uk/pdbsum/7k1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k1v ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/I6X8R2_MYCTU I6X8R2_MYCTU]
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Zinc metalloprotease 1 (Zmp1), a Mycobacterium tuberculosis 75 kDa secreted enzyme, mediates key stages of tuberculosis disease progression. The biological activity of Zmp1 presumably stems from its ability to degrade bacterium- and/or host-derived peptides. The crystal structures of Zmp1 and related M13 metalloproteases, such as neprilysin and endothelin-converting enzyme-1 were determined only in the closed conformation, which cannot capture substrates or release proteolytic products. Thus, the mechanisms of substrate binding and selectivity remain elusive. Here we report two open-state cryo-EM structures of Zmp1, revealed by our SAXS analysis to be the dominant states in solution. Our structural analyses reveal how ligand binding induces a conformational switch in four linker regions to drive the rigid body motion of the D1 and D2 domains, which form the sizable catalytic chamber. Furthermore, they offer insights into the catalytic cycle and mechanism of substrate recognition of M13 metalloproteases for future therapeutic innovations.
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Structural analysis of Mycobacteriumtuberculosis M13 metalloprotease Zmp1 open states.,Liang WG, Mancl JM, Zhao M, Tang WJ Structure. 2020 Dec 22. pii: S0969-2126(20)30469-X. doi:, 10.1016/j.str.2020.12.002. PMID:33378640<ref>PMID:33378640</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7k1v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myctu]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Liang, W G]]
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[[Category: Liang WG]]
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[[Category: Mancl, J M]]
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[[Category: Mancl JM]]
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[[Category: Tang, W]]
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[[Category: Tang W]]
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[[Category: Zhao, M]]
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[[Category: Zhao M]]
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[[Category: Hydrolase]]
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[[Category: Open state]]
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Current revision

Partial open state of Mycobacterium tuberculosis zinc metalloprotease 1

PDB ID 7k1v

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OCA

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