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2e85
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2e85" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e85, resolution 1.70Å" /> '''Crystal Structure of...) |
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| - | [[Image:2e85.jpg|left|200px]]<br /><applet load="2e85" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2e85, resolution 1.70Å" /> | ||
| - | '''Crystal Structure of the Hydrogenase 3 Maturation protease'''<br /> | ||
| - | == | + | ==Crystal Structure of the Hydrogenase 3 Maturation protease== |
| - | + | <StructureSection load='2e85' size='340' side='right'caption='[[2e85]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2e85]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E85 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=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=2e85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e85 OCA], [https://pdbe.org/2e85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e85 RCSB], [https://www.ebi.ac.uk/pdbsum/2e85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e85 ProSAT], [https://www.topsan.org/Proteins/RSGI/2e85 TOPSAN]</span></td></tr> | |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/HYCI_ECOLI HYCI_ECOLI] Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3. | |
| - | [[ | + | == 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/e8/2e85_consurf.spt"</scriptWhenChecked> |
| - | [[ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2e85 ConSurf]. |
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The maturation of [NiFe]-hydrogenases is a catalyzed process involving the activities of at least seven proteins. The last step consists of the endoproteolytic cleavage of the precursor of the large subunit, after the [NiFe]-metal center has been assembled. The HycI endopeptidase is involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3 from Escherichia coli. Although HycI has been well characterized biochemically, the crystallization of the protein has been quite challenging. Here, we present the crystal structure of HycI at 1.70 A resolution. The crystal structure resembles the recently reported solution structure (NMR) of the same protein and the holo-HyPD structure of the same family, but a significant conformational change is observed at the L5 loop, as compared with the solution structures of HycI and HyPD. In our crystal structure, three specific metal binding sites (Ca1-3) were identified and these metal ions are possibly involved in the C-terminal cleavage of HycE. | ||
| - | + | Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli.,Kumarevel T, Tanaka T, Bessho Y, Shinkai A, Yokoyama S Biochem Biophys Res Commun. 2009 Nov 13;389(2):310-4. Epub 2009 Aug 29. PMID:19720045<ref>PMID:19720045</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2e85" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kumarevel TS]] | ||
| + | [[Category: Shinkai A]] | ||
| + | [[Category: Tanaka T]] | ||
| + | [[Category: Yokoyama S]] | ||
Current revision
Crystal Structure of the Hydrogenase 3 Maturation protease
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