1mbx

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(New page: 200px<br /><applet load="1mbx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mbx, resolution 2.25&Aring;" /> '''CRYSTAL STRUCTURE AN...)
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[[Image:1mbx.gif|left|200px]]<br /><applet load="1mbx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mbx, resolution 2.25&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND==
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Substrate selectivity and proteolytic activity for the E. coli, ATP-dependent protease, ClpAP, is modulated by an adaptor protein, ClpS., ClpS binds to ClpA, the regulatory component of the ClpAP complex. We, report the crystal structure of ClpS in complex with the isolated, N-terminal domain of ClpA in two different crystal forms at 2.3- and 3.3-A, resolution. The ClpS structure forms an alpha/beta-sandwich and is, topologically analogous to the C-terminal domain of the ribosomal protein, L7/L12. ClpS contacts two surfaces on the N-terminal domain in both, crystal forms; the more extensive interface was shown to be favored in, solution by protease protection experiments. The N-terminal 20 residues of, ClpS are not visible in the crystal structures; the removal of the first, 17 residues produces ClpSDeltaN, which binds to the ClpA N-domain but no, longer inhibits ClpA activity. A zinc binding site involving two His and, one Glu residue was identified crystallographically in the N-terminal, domain of ClpA. In a model of ClpS bound to hexameric ClpA, ClpS is, oriented with its N terminus directed toward the distal surface of ClpA, suggesting that the N-terminal region of ClpS may affect productive, substrate interactions at the apical surface or substrate entry into the, ClpA translocation channel.
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<StructureSection load='1mbx' size='340' side='right'caption='[[1mbx]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mbx]] is a 4 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=1MBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBX 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]] 2.25&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=YBT:BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE+YTTRIUM'>YBT</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=1mbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbx OCA], [https://pdbe.org/1mbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbx RCSB], [https://www.ebi.ac.uk/pdbsum/1mbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPA_ECOLI CLPA_ECOLI] ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.
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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/mb/1mbx_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=1mbx ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MBX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL, ZN, YBT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MBX OCA].
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA., Guo F, Esser L, Singh SK, Maurizi MR, Xia D, J Biol Chem. 2002 Nov 29;277(48):46753-62. Epub 2002 Sep 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12235156 12235156]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Esser, L.]]
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[[Category: Esser L]]
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[[Category: Guo, F.]]
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[[Category: Guo F]]
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[[Category: Maurizi, M.R.]]
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[[Category: Maurizi MR]]
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[[Category: Singh, S.K.]]
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[[Category: Singh SK]]
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[[Category: Xia, D.]]
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[[Category: Xia D]]
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[[Category: CL]]
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[[Category: GOL]]
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[[Category: YBT]]
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[[Category: ZN]]
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[[Category: aaa+ family]]
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[[Category: adaptors]]
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[[Category: atp-dependent protease]]
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[[Category: hsp100/clp chaperone]]
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[[Category: protein binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:19:07 2007''
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND

PDB ID 1mbx

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