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1mg9

From Proteopedia

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[[Image:1mg9.jpg|left|200px]]
 
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{{Structure
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==The structural basis of ClpS-mediated switch in ClpA substrate recognition==
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|PDB= 1mg9 |SIZE=350|CAPTION= <scene name='initialview01'>1mg9</scene>, resolution 2.30&Aring;
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<StructureSection load='1mg9' size='340' side='right'caption='[[1mg9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SPK:SPERMINE (FULLY PROTONATED FORM)'>SPK</scene>
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<table><tr><td colspan='2'>[[1mg9]] 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=1MG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MG9 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPK:SPERMINE+(FULLY+PROTONATED+FORM)'>SPK</scene></td></tr>
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}}
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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=1mg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mg9 OCA], [https://pdbe.org/1mg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mg9 RCSB], [https://www.ebi.ac.uk/pdbsum/1mg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mg9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPS_ECOLI CLPS_ECOLI] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
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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/mg/1mg9_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=1mg9 ConSurf].
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<div style="clear:both"></div>
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'''The structural basis of ClpS-mediated switch in ClpA substrate recognition'''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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__TOC__
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==Overview==
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</StructureSection>
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In Escherichia coli, protein degradation is performed by several proteolytic machines, including ClpAP. Generally, the substrate specificity of these machines is determined by chaperone components, such as ClpA. In some cases, however, the specificity is modified by adaptor proteins, such as ClpS. Here we report the 2.5 A resolution crystal structure of ClpS in complex with the N-terminal domain of ClpA. Using mutagenesis, we demonstrate that two contact residues (Glu79 and Lys 84) are essential not only for ClpAS complex formation but also for ClpAPS-mediated substrate degradation. The corresponding residues are absent in the chaperone ClpB, providing a structural rationale for the unique specificity shown by ClpS despite the high overall similarity between ClpA and ClpB. To determine the location of ClpS within the ClpA hexamer, we modeled the N-terminal domain of ClpA onto a structurally defined, homologous AAA+ protein. From this model, we proposed a molecular mechanism to explain the ClpS-mediated switch in ClpA substrate specificity.
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==About this Structure==
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1MG9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MG9 OCA].
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==Reference==
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Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA., Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA, Nat Struct Biol. 2002 Dec;9(12):906-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12426582 12426582]
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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: Bukau, B.]]
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[[Category: Bukau B]]
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[[Category: Cusack, S.]]
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[[Category: Cusack S]]
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[[Category: Dougan, D A.]]
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[[Category: Dougan DA]]
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[[Category: Paal, K.]]
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[[Category: Paal K]]
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[[Category: Ravelli, R B.]]
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[[Category: Ravelli RB]]
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[[Category: Zeth, K.]]
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[[Category: Zeth K]]
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[[Category: SPK]]
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[[Category: aaa+atpase]]
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[[Category: substrate sensor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:43:10 2008''
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Current revision

The structural basis of ClpS-mediated switch in ClpA substrate recognition

PDB ID 1mg9

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