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3jtn

From Proteopedia

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{{STRUCTURE_3jtn| PDB=3jtn | SCENE= }}
 
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===Crystal Structure of the c-terminal domain of YpbH===
 
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{{ABSTRACT_PUBMED_019801546}}
 
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==Function==
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==Crystal Structure of the c-terminal domain of YpbH==
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[[http://www.uniprot.org/uniprot/MECA2_BACSU MECA2_BACSU]] Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Also involved in Spx degradation by ClpC (By similarity). Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation.<ref>PMID:11914365</ref>
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<StructureSection load='3jtn' size='340' side='right'caption='[[3jtn]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[3jtn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JTN FirstGlance]. <br>
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[[3jtn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JTN 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]] 2.09&#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=IOD:IODIDE+ION'>IOD</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=3jtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jtn OCA], [https://pdbe.org/3jtn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jtn RCSB], [https://www.ebi.ac.uk/pdbsum/3jtn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jtn ProSAT]</span></td></tr>
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<references group="xtra"/><references/>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MECA2_BACSU MECA2_BACSU] Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Also involved in Spx degradation by ClpC (By similarity). Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation.<ref>PMID:11914365</ref>
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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/jt/3jtn_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=3jtn ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Mei, Z.]]
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[[Category: Large Structures]]
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[[Category: Qi, Y.]]
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[[Category: Mei Z]]
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[[Category: Shi, Y.]]
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[[Category: Qi Y]]
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[[Category: Wang, F.]]
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[[Category: Shi Y]]
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[[Category: Wang, J.]]
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[[Category: Wang F]]
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[[Category: Yan, C.]]
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[[Category: Wang J]]
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[[Category: Adaptor protein]]
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[[Category: Yan C]]
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[[Category: Competence]]
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[[Category: Protein binding]]
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[[Category: Sporulation]]
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[[Category: Ypbh]]
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Current revision

Crystal Structure of the c-terminal domain of YpbH

PDB ID 3jtn

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OCA

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