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1r6v

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(New page: 200px<br /><applet load="1r6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6v, resolution 1.7&Aring;" /> '''Crystal structure of ...)
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[[Image:1r6v.gif|left|200px]]<br /><applet load="1r6v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1r6v, resolution 1.7&Aring;" />
 
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'''Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin'''<br />
 
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==Overview==
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==Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin==
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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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<StructureSection load='1r6v' size='340' side='right'caption='[[1r6v]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1R6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fervidobacterium_pennivorans Fervidobacterium pennivorans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R6V OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<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>
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==Reference==
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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=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>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14687574 14687574]
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r6/1r6v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Fervidobacterium pennivorans]]
[[Category: Fervidobacterium pennivorans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Kim, J.S.]]
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[[Category: Kim JS]]
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[[Category: Kluskens, L.D.]]
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[[Category: Kluskens LD]]
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[[Category: Oost, J.van.der.]]
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[[Category: De Vos WM]]
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[[Category: Vos, W.M.de.]]
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[[Category: Van der Oost J]]
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[[Category: CA]]
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[[Category: propeptide]]
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[[Category: sandwich domain]]
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[[Category: subtilisin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:15:27 2007''
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Current revision

Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin

PDB ID 1r6v

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