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1mg9

From Proteopedia

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Revision as of 06:24, 31 January 2018

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

Structural highlights

1mg9 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1lzw
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CLPS_ECOLI] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. [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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:12426582^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA. Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat Struct Biol. 2002 Dec;9(12):906-11. PMID:12426582 doi:10.1038/nsb869

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mg9"

@@ Line 1: / Line 1: @@
 ==The structural basis of ClpS-mediated switch in ClpA substrate recognition==
 <StructureSection load='1mg9' size='340' side='right' caption='[[1mg9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SPK:SPERMINE+(FULLY+PROTONATED+FORM)'>SPK</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lzw|1lzw]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mg9 OCA], [http://pdbe.org/1mg9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mg9 RCSB], [http://www.ebi.ac.uk/pdbsum/1mg9 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mg9 OCA], [http://pdbe.org/1mg9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mg9 RCSB], [http://www.ebi.ac.uk/pdbsum/1mg9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mg9 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mg/1mg9_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mg/1mg9_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1mg9" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Clp Protease|Clp Protease]]
 == References ==
 <references/>

1mg9

From Proteopedia

Revision as of 06:24, 31 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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