7esi: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==Crystal structure of the collagenase unit of a Vibrio collagenase from Vibrio harveyi VHJR7 at 1. 8 angstrom resolution.== | ||
<StructureSection load='7esi' size='340' side='right'caption='[[7esi]]' scene=''> | <StructureSection load='7esi' size='340' side='right'caption='[[7esi]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7esi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi_VHJR7 Vibrio harveyi VHJR7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ESI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ESI FirstGlance]. <br> | ||
</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=7esi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7esi OCA], [https://pdbe.org/7esi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7esi RCSB], [https://www.ebi.ac.uk/pdbsum/7esi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7esi ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7esi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7esi OCA], [https://pdbe.org/7esi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7esi RCSB], [https://www.ebi.ac.uk/pdbsum/7esi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7esi ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A8B3DGT3_VIBHA A0A8B3DGT3_VIBHA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The collagenases of Vibrio species, many of which are pathogens, have been regarded as an important virulence factor. However, there is little information on the structure and collagenolytic mechanism of Vibrio collagenase. Here, we report the crystal structure of the collagenase module (CM) of Vibrio collagenase VhaC and the conformation of VhaC in solution. Structural and biochemical analyses and molecular dynamics studies reveal that triple-helical collagen is initially recognized by the activator domain, followed by subsequent cleavage by the peptidase domain along with the closing movement of CM. This is different from the peptidolytic mode or the proposed collagenolysis of Clostridium collagenase. We propose a model for the integrated collagenolytic mechanism of VhaC, integrating the functions of VhaC accessory domains and its collagen degradation pattern. This study provides insight into the mechanism of bacterial collagenolysis and helps in structure-based drug design targeting of the Vibrio collagenase. | |||
Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.,Wang Y, Wang P, Cao HY, Ding HT, Su HN, Liu SC, Liu G, Zhang X, Li CY, Peng M, Li F, Li S, Chen Y, Chen XL, Zhang YZ Nat Commun. 2022 Jan 28;13(1):566. doi: 10.1038/s41467-022-28264-1. PMID:35091565<ref>PMID:35091565</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7esi" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Collagenase 3D structures|Collagenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vibrio harveyi VHJR7]] | ||
[[Category: Cao HY]] | |||
[[Category: Peng M]] | |||
[[Category: Wang Y]] | |||
[[Category: Zhang YZ]] | |||
Revision as of 15:52, 22 February 2023
Crystal structure of the collagenase unit of a Vibrio collagenase from Vibrio harveyi VHJR7 at 1. 8 angstrom resolution.Crystal structure of the collagenase unit of a Vibrio collagenase from Vibrio harveyi VHJR7 at 1. 8 angstrom resolution.
Structural highlights
FunctionPublication Abstract from PubMedThe collagenases of Vibrio species, many of which are pathogens, have been regarded as an important virulence factor. However, there is little information on the structure and collagenolytic mechanism of Vibrio collagenase. Here, we report the crystal structure of the collagenase module (CM) of Vibrio collagenase VhaC and the conformation of VhaC in solution. Structural and biochemical analyses and molecular dynamics studies reveal that triple-helical collagen is initially recognized by the activator domain, followed by subsequent cleavage by the peptidase domain along with the closing movement of CM. This is different from the peptidolytic mode or the proposed collagenolysis of Clostridium collagenase. We propose a model for the integrated collagenolytic mechanism of VhaC, integrating the functions of VhaC accessory domains and its collagen degradation pattern. This study provides insight into the mechanism of bacterial collagenolysis and helps in structure-based drug design targeting of the Vibrio collagenase. Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.,Wang Y, Wang P, Cao HY, Ding HT, Su HN, Liu SC, Liu G, Zhang X, Li CY, Peng M, Li F, Li S, Chen Y, Chen XL, Zhang YZ Nat Commun. 2022 Jan 28;13(1):566. doi: 10.1038/s41467-022-28264-1. PMID:35091565[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||