2cki
From Proteopedia
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| - | [[Image:2cki.gif|left|200px]]<br /><applet load="2cki" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cki, resolution 1.70Å" /> | ||
| - | '''STRUCTURE OF ULILYSIN, A MEMBER OF THE PAPPALYSIN FAMILY OF METZINCIN METALLOENDOPEPTIDASES.'''<br /> | ||
| - | == | + | ==Structure of Ulilysin, a member of the pappalysin family of metzincin metalloendopeptidases.== |
| + | <StructureSection load='2cki' size='340' side='right'caption='[[2cki]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2cki]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKI FirstGlance]. <br> | ||
| + | </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=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</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=2cki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cki OCA], [https://pdbe.org/2cki PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cki RCSB], [https://www.ebi.ac.uk/pdbsum/2cki PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cki ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/2cki_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2cki ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The metzincin clan encompasses several families of zinc-dependent metalloproteases with proven function both in physiology and pathology. They act either as broad spectrum protein degraders or as sheddases, operating through limited proteolysis. Among the structurally uncharacterized metzincin families are the pappalysins, of which the most thoroughly studied member is human pregnancy-associated plasma protein A (PAPP-A), a heavily glycosylated 170-kDa multidomain protein specifically cleaving insulin-like growth factor (IGF)-binding proteins (IGFBPs). Proulilysin is a 38-kDa archaeal protein that shares sequence similarity with PAPP-A but encompasses only the pro-domain and the catalytic domain. It undergoes calcium-mediated autolytic activation, and the mature protein adopts a three-dimensional structure with two subdomains separated by an active site cleft containing the catalytic zinc ion. This structure is reminiscent of human members of the adamalysin/ADAMs (a disintegrin and a metalloprotease) family of metzincins. A bound dipeptide yields information on the substrate specificity of ulilysin, which specifically hydrolyzes IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Accordingly, ulilysin has higher proteolytic efficiency and a broader substrate specificity than human PAPP-A. The structure of ulilysin represents a prototype for the catalytic domain of pappalysins. | The metzincin clan encompasses several families of zinc-dependent metalloproteases with proven function both in physiology and pathology. They act either as broad spectrum protein degraders or as sheddases, operating through limited proteolysis. Among the structurally uncharacterized metzincin families are the pappalysins, of which the most thoroughly studied member is human pregnancy-associated plasma protein A (PAPP-A), a heavily glycosylated 170-kDa multidomain protein specifically cleaving insulin-like growth factor (IGF)-binding proteins (IGFBPs). Proulilysin is a 38-kDa archaeal protein that shares sequence similarity with PAPP-A but encompasses only the pro-domain and the catalytic domain. It undergoes calcium-mediated autolytic activation, and the mature protein adopts a three-dimensional structure with two subdomains separated by an active site cleft containing the catalytic zinc ion. This structure is reminiscent of human members of the adamalysin/ADAMs (a disintegrin and a metalloprotease) family of metzincins. A bound dipeptide yields information on the substrate specificity of ulilysin, which specifically hydrolyzes IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Accordingly, ulilysin has higher proteolytic efficiency and a broader substrate specificity than human PAPP-A. The structure of ulilysin represents a prototype for the catalytic domain of pappalysins. | ||
| - | + | Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases.,Tallant C, Garcia-Castellanos R, Seco J, Baumann U, Gomis-Ruth FX J Biol Chem. 2006 Jun 30;281(26):17920-8. Epub 2006 Apr 20. PMID:16627477<ref>PMID:16627477</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2cki" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Baumann | + | <references/> |
| - | [[Category: Garcia-Castellanos | + | __TOC__ |
| - | [[Category: Gomis-Ruth | + | </StructureSection> |
| - | [[Category: Seco | + | [[Category: Large Structures]] |
| - | [[Category: Tallant | + | [[Category: Methanosarcina acetivorans C2A]] |
| - | + | [[Category: Baumann U]] | |
| - | + | [[Category: Garcia-Castellanos R]] | |
| - | + | [[Category: Gomis-Ruth FX]] | |
| - | + | [[Category: Seco J]] | |
| - | + | [[Category: Tallant C]] | |
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Current revision
Structure of Ulilysin, a member of the pappalysin family of metzincin metalloendopeptidases.
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