1r6v
From Proteopedia
(Difference between revisions)
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<StructureSection load='1r6v' size='340' side='right'caption='[[1r6v]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1r6v' size='340' side='right'caption='[[1r6v]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1r6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1r6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fervidobacterium_pennivorans Fervidobacterium pennivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R6V FirstGlance]. <br> |
| - | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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></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=1r6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6v OCA], [https://pdbe.org/1r6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6v RCSB], [https://www.ebi.ac.uk/pdbsum/1r6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6v 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=1r6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6v OCA], [https://pdbe.org/1r6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6v RCSB], [https://www.ebi.ac.uk/pdbsum/1r6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FLS_FERPE FLS_FERPE] Protease able to degrade keratin into peptides. Is responsible for keratinolysis by F.pennivorans, which allows this bacterium to grow on native feathers.<ref>PMID:16535379</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r6v ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r6v ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Structure-forming fibrous proteins like keratins, gelatins and collagens are degraded only by a few proteases as their tight packing limits access to the potential cleavage sites. To understand the keratin degradation in detail, we describe the first crystal structure of a keratin-degrading enzyme (keratinase), fervidolysin, from Fervidobacterium pennivorans as an immature form with propeptide (PD)-bound. The 1.7A resolution crystal structure shows that the protease is composed of four domains: a catalytic domain (CD), two beta-sandwich domains (SDs), and the PD domain. A structural alignment shows a distant relationship between the PD-CD substructure of fervidolysin and pro-subtilisin E. Tight binding of PD to the remaining part of the protease is mediated by hydrogen bonds along the domain surfaces and around the active cleft, and by the clamps to SD1 and SD2. The crystal structure of this multi-domain protein fervidolysin provides insights into proenzyme activation and the role of non-catalytic domains, suggesting a functional relationship to the fibronectin (FN)-like domains of the human promatrix metalloprotease-2 (proMMP-2) that degrades the fibrous polymeric substrate gelatin. | ||
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| - | Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin.,Kim JS, Kluskens LD, de Vos WM, Huber R, van der Oost J J Mol Biol. 2004 Jan 16;335(3):787-97. PMID:14687574<ref>PMID:14687574</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1r6v" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Fervidobacterium pennivorans]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Huber | + | [[Category: Huber R]] |
| - | [[Category: Kim | + | [[Category: Kim JS]] |
| - | [[Category: Kluskens | + | [[Category: Kluskens LD]] |
| - | + | [[Category: De Vos WM]] | |
| - | [[Category: Vos | + | [[Category: Van der Oost J]] |
| - | [[Category: | + | |
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Current revision
Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin
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