2ds5

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(New page: 200px<br /><applet load="2ds5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ds5, resolution 1.5&Aring;" /> '''Structure of the ZBD ...)
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[[Image:2ds5.gif|left|200px]]<br /><applet load="2ds5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ds5, resolution 1.5&Aring;" />
 
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'''Structure of the ZBD in the orthorhomibic crystal from'''<br />
 
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==Overview==
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==Structure of the ZBD in the orthorhomibic crystal from==
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The degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial, cytosol is carried out by the ClpXP protease and is markedly stimulated by, the SspB adaptor protein. It has previously been reported that the, amino-terminal zinc-binding domain of ClpX (ZBD) is involved in complex, formation with the SspB-tail (XB: ClpX-binding motif). In an effort to, better understand the recognition of SspB by ClpX and the mechanism of, delivery of ssrA-tagged substrates to ClpXP, we have determined the, structures of ZBD alone at 1.5, 2.0, and 2.5 A resolution in each, different crystal form and also in complex with XB peptide at 1.6 A, resolution. The XB peptide forms an antiparallel beta-sheet with two, beta-strands of ZBD, and the structure shows a 1:1 stoichiometric complex, between ZBD and XB, suggesting that there are two independent, SspB-tail-binding sites in ZBD. The high-resolution ZBD:XB complex, structure, in combination with biochemical analyses, can account for key, determinants in the recognition of the SspB-tail by ClpX and sheds light, on the mechanism of delivery of target proteins to the prokaryotic, degradation machine.
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<StructureSection load='2ds5' size='340' side='right'caption='[[2ds5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ds5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DS5 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]] 1.5&#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=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=2ds5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ds5 OCA], [https://pdbe.org/2ds5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ds5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ds5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ds5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPX_ECOLI CLPX_ECOLI] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175]
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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/ds/2ds5_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=2ds5 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 degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial cytosol is carried out by the ClpXP protease and is markedly stimulated by the SspB adaptor protein. It has previously been reported that the amino-terminal zinc-binding domain of ClpX (ZBD) is involved in complex formation with the SspB-tail (XB: ClpX-binding motif). In an effort to better understand the recognition of SspB by ClpX and the mechanism of delivery of ssrA-tagged substrates to ClpXP, we have determined the structures of ZBD alone at 1.5, 2.0, and 2.5 A resolution in each different crystal form and also in complex with XB peptide at 1.6 A resolution. The XB peptide forms an antiparallel beta-sheet with two beta-strands of ZBD, and the structure shows a 1:1 stoichiometric complex between ZBD and XB, suggesting that there are two independent SspB-tail-binding sites in ZBD. The high-resolution ZBD:XB complex structure, in combination with biochemical analyses, can account for key determinants in the recognition of the SspB-tail by ClpX and sheds light on the mechanism of delivery of target proteins to the prokaryotic degradation machine.
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==About this Structure==
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Structural basis of SspB-tail recognition by the zinc binding domain of ClpX.,Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK J Mol Biol. 2007 Mar 23;367(2):514-26. Epub 2007 Jan 9. PMID:17258768<ref>PMID:17258768</ref>
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2DS5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, CA and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DS5 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural Basis of SspB-tail Recognition by the Zinc Binding Domain of ClpX., Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK, J Mol Biol. 2007 Mar 23;367(2):514-26. Epub 2007 Jan 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17258768 17258768]
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</div>
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<div class="pdbe-citations 2ds5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hong, S.B.]]
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[[Category: Hong SB]]
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[[Category: Lee, B.G.]]
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[[Category: Lee BG]]
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[[Category: Park, E.Y.]]
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[[Category: Park EY]]
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[[Category: Song, H.K.]]
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[[Category: Song HK]]
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[[Category: CA]]
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[[Category: PG4]]
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[[Category: ZN]]
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[[Category: treble cleft zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:45:06 2007''
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Current revision

Structure of the ZBD in the orthorhomibic crystal from

PDB ID 2ds5

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