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1k7q

From Proteopedia

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[[Image:1k7q.jpg|left|200px]]
 
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{{Structure
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==PrtC from Erwinia chrysanthemi: E189A mutant==
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|PDB= 1k7q |SIZE=350|CAPTION= <scene name='initialview01'>1k7q</scene>, resolution 1.80&Aring;
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<StructureSection load='1k7q' size='340' side='right'caption='[[1k7q]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1k7q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K7Q FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.8&#8491;</td></tr>
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|GENE= prtC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi])
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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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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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=1k7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k7q OCA], [https://pdbe.org/1k7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k7q RCSB], [https://www.ebi.ac.uk/pdbsum/1k7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k7q ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1go7|1GO7]], [[1go8|1GO8]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k7q OCA], [http://www.ebi.ac.uk/pdbsum/1k7q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k7q RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PRTC_DICCH PRTC_DICCH]
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== Evolutionary Conservation ==
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'''PrtC from Erwinia chrysanthemi: E189A mutant'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/1k7q_consurf.spt"</scriptWhenChecked>
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PrtC, a metallo-protease secreted by Erwinia chrysanthemi, is a member of the serralysin family and hence belongs to the metzincin superfamily. While the crystal structures of representatives of all metzincin subfamilies have been elucidated in the past, there is still some controversy about the reaction mechanism and the role of certain characteristic amino acids in the active centre. In this study, we probed the role of Tyr228 and Glu189 by site-directed mutagenesis and X-ray crystallography. There is evidence that these residues participate in catalysis, although conflicting hypotheses have been proposed. The crystal structures of wild-type and mutants have been refined to an R(free) of about 0.20 at resolutions of 2.0 A or better. Exchange of Glu189 versus alanine reduces the catalytic efficiency to less than 0.5 % using resorufin casein as substrate and to about 3 % using an assay utilising the thiol ester Ac-Pro-Leu-Gly-[(S)Leu]-Leu-Gly-OEt. The drop in activity is caused by a reduction in k(cat) while the K(M) values are virtually the same. In the resorufin casein assay, the mutant Y228F shows about 3 % of the wild-type activity and in the thiol ester assay this increases to about 56 %. In the latter case, the K(M) value of the mutant is increased from 5.3 mM to 9.0 mM with only little reduction in k(cat). The different behaviour of this mutant with respect to the two substrates can be explained by a switch in the rate-determining step during catalysis. The study presented here provides clear evidence that Glu189 of the HEXXHXXGXXH motif is the catalytic base, while Tyr228 is more likely involved in substrate binding and the stabilisation of the tetrahedral transition state.
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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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==About this Structure==
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</jmolCheckbox>
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1K7Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K7Q OCA].
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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=1k7q ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Protease C of Erwinia chrysanthemi: the crystal structure and role of amino acids Y228 and E189., Hege T, Baumann U, J Mol Biol. 2001 Nov 23;314(2):187-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11718553 11718553]
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</StructureSection>
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[[Category: Erwinia chrysanthemi]]
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[[Category: Dickeya chrysanthemi]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baumann, U.]]
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[[Category: Baumann U]]
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[[Category: Hege, T.]]
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[[Category: Hege T]]
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[[Category: hydrolase]]
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[[Category: metalloprotease]]
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[[Category: protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:34 2008''
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Current revision

PrtC from Erwinia chrysanthemi: E189A mutant

PDB ID 1k7q

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