3hbv

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[[Image:3hbv.png|left|200px]]
 
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{{STRUCTURE_3hbv| PDB=3hbv | SCENE= }}
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==PrtC methionine mutants: M226A in-house==
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<StructureSection load='3hbv' size='340' side='right'caption='[[3hbv]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3hbv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HBV FirstGlance]. <br>
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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]] 1.95&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=3hbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hbv OCA], [https://pdbe.org/3hbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hbv RCSB], [https://www.ebi.ac.uk/pdbsum/3hbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hbv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRTC_DICCH PRTC_DICCH]
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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/hb/3hbv_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/main_output.php?pdb_ID=3hbv 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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Abstract The metzincins constitute a subclan of metalloproteases possessing a HEXXHXXGXXH/D zinc-binding consensus sequence where the three histidines are zinc ligands and the glutamic acid the catalytic base. A completely conserved methionine is located downstream of this motif. Families of the metzincin clan comprise, besides others, astacins, ADAMS proteases, matrix metalloproteases and serralysins. The latter are extracellular 50 kDa proteases secreted by Gram-negative bacteria via a type I secretion system. While there is a large body of structural and biochemical information available, the function of the conserved methionine has not been convincingly clarified yet. Here we present the crystal structures of a number of mutants of the serralysin member protease C with the conserved methionine being replaced by Ile, Ala and His. Together with our former report on the leucine and cysteine mutants, we demonstrate here that replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the chi(2) angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain.
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===PrtC methionine mutants: M226A in-house===
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Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site.,Oberholzer AE, Bumann M, Hege T, Russo S, Baumann U Biol Chem. 2009 Jun 27. PMID:19558324<ref>PMID:19558324</ref>
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{{ABSTRACT_PUBMED_19558324}}
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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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==About this Structure==
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<div class="pdbe-citations 3hbv" style="background-color:#fffaf0;"></div>
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[[3hbv]] is a 2 chain structure with 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=3HBV OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:019558324</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Erwinia chrysanthemi]]
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[[Category: Dickeya chrysanthemi]]
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[[Category: Baumann, U.]]
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[[Category: Large Structures]]
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[[Category: Bumann, M.]]
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[[Category: Unidentified]]
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[[Category: Hege, T.]]
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[[Category: Baumann U]]
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[[Category: Oberholzer, A E.]]
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[[Category: Bumann M]]
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[[Category: Russo, S.]]
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[[Category: Hege T]]
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[[Category: Beta roll]]
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[[Category: Oberholzer AE]]
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[[Category: Hydrolase]]
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[[Category: Russo S]]
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[[Category: Met-turn]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Metzincin]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Zymogen]]
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Current revision

PrtC methionine mutants: M226A in-house

PDB ID 3hbv

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