1k7i

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(New page: 200px<br /><applet load="1k7i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k7i, resolution 1.59&Aring;" /> '''PrtC from Erwinia ch...)
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[[Image:1k7i.jpg|left|200px]]<br /><applet load="1k7i" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k7i, resolution 1.59&Aring;" />
 
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'''PrtC from Erwinia chrysanthemi: Y228F mutant'''<br />
 
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==Overview==
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==PrtC from Erwinia chrysanthemi: Y228F mutant==
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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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<StructureSection load='1k7i' size='340' side='right'caption='[[1k7i]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1k7i]] 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=1K7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K7I FirstGlance]. <br>
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1K7I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K7I 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]] 1.59&#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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1k7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k7i OCA], [https://pdbe.org/1k7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k7i RCSB], [https://www.ebi.ac.uk/pdbsum/1k7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k7i ProSAT]</span></td></tr>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11718553 11718553]
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</table>
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[[Category: Erwinia chrysanthemi]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/PRTC_DICCH PRTC_DICCH]
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[[Category: Baumann, U.]]
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== Evolutionary Conservation ==
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[[Category: Hege, T.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: CA]]
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Check<jmol>
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[[Category: ZN]]
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<jmolCheckbox>
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[[Category: hydrolase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/1k7i_consurf.spt"</scriptWhenChecked>
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[[Category: metalloprotease]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: protease]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:55:21 2007''
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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=1k7i ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Dickeya chrysanthemi]]
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[[Category: Large Structures]]
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[[Category: Baumann U]]
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[[Category: Hege T]]

Current revision

PrtC from Erwinia chrysanthemi: Y228F mutant

PDB ID 1k7i

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