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2e85

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[[Image:2e85.png|left|200px]]
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==Crystal Structure of the Hydrogenase 3 Maturation protease==
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<StructureSection load='2e85' size='340' side='right' caption='[[2e85]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2e85]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E85 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e85 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e85 RCSB], [http://www.ebi.ac.uk/pdbsum/2e85 PDBsum], [http://www.topsan.org/Proteins/RSGI/2e85 TOPSAN]</span></td></tr>
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<table>
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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/e8/2e85_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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2e85| PDB=2e85 | SCENE= }}
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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>
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===Crystal Structure of the Hydrogenase 3 Maturation protease===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_19720045}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2e85]] is a 2 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:019720045</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Kumarevel, T S.]]
[[Category: Kumarevel, T S.]]

Revision as of 03:05, 30 September 2014

Crystal Structure of the Hydrogenase 3 Maturation protease

2e85, resolution 1.70Å

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