1r6o: Difference between revisions

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<StructureSection load='1r6o' size='340' side='right'caption='[[1r6o]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='1r6o' size='340' side='right'caption='[[1r6o]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1r6o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R6O FirstGlance]. <br>
<table><tr><td colspan='2'>[[1r6o]] 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=1R6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R6O FirstGlance]. <br>
</td></tr><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=Y1:YTTRIUM+ION'>Y1</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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r6b|1r6b]], [[1r6c|1r6c]], [[1r6q|1r6q]]</div></td></tr>
<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=Y1:YTTRIUM+ION'>Y1</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLPA, LOPD, B0882, C1019, Z1119, ECS0968 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), CLPS, B0881, C1018, Z1118, ECS0967, SF0841, S0881 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6o OCA], [https://pdbe.org/1r6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6o RCSB], [https://www.ebi.ac.uk/pdbsum/1r6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6o ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6o OCA], [http://pdbe.org/1r6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r6o RCSB], [http://www.ebi.ac.uk/pdbsum/1r6o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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. [[http://www.uniprot.org/uniprot/CLPS_ECOLI CLPS_ECOLI]] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.  
[https://www.uniprot.org/uniprot/CLPS_ECOLI CLPS_ECOLI] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1r6o ConSurf].
</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=1r6o ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in the dissolution and degradation of regulatory proteins and protein aggregates. ClpA consists of three functional domains: an N-terminal domain and two ATPase domains, D1 and D2. The N-domain is attached to D1 by a mobile linker and is made up of two tightly bound, identically folded alpha-helical bundles related by a pseudo 2-fold symmetry. Between the halves of the pseudo-dimer is a large flexible acidic loop that becomes better ordered upon binding of the small adaptor protein, ClpS. We have identified a number of structural features in the N-domain, including a Zn(++) binding motif, several interfaces for binding to ClpS, and a prominent hydrophobic surface area that binds peptides in different configurations. These structural motifs may contribute to binding of protein or peptide substrates with weak affinity and broad specificity. Kinetic studies comparing wild-type ClpA to a mutant ClpA with its N-domain deleted show that the N-domains contribute to the binding of a non-specific protein substrate but not of a folded substrate with the specific SsrA recognition tag. A functional model is proposed in which the N-domains in ClpA function as tentacles to weakly hold on to proteins thereby enhancing local substrate concentration.
Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.,Xia D, Esser L, Singh SK, Guo F, Maurizi MR J Struct Biol. 2004 Apr-May;146(1-2):166-79. PMID:15037248<ref>PMID:15037248</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1r6o" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ATP-dependent Clp protease adaptor protein 3D structures|ATP-dependent Clp protease adaptor protein 3D structures]]
*[[ATP-dependent Clp protease adaptor protein 3D structures|ATP-dependent Clp protease adaptor protein 3D structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Esser, L]]
[[Category: Esser L]]
[[Category: Guo, F]]
[[Category: Guo F]]
[[Category: Maurizi, M R]]
[[Category: Maurizi MR]]
[[Category: Singh, S K]]
[[Category: Singh SK]]
[[Category: Xia, D]]
[[Category: Xia D]]
[[Category: Aaa+]]
[[Category: Binding mechanism]]
[[Category: Clp]]
[[Category: Clpa]]
[[Category: Crystal]]
[[Category: Hydrolase]]
[[Category: N-terminal domain]]

Latest revision as of 11:20, 14 February 2024

ATP-dependent Clp protease ATP-binding subunit clpA/ATP-dependent Clp protease adaptor protein clpSATP-dependent Clp protease ATP-binding subunit clpA/ATP-dependent Clp protease adaptor protein clpS

Structural highlights

1r6o is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:, , , ,
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.

Evolutionary Conservation

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

See Also

1r6o, resolution 2.25Å

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