1r6c

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[[Image:1r6c.gif|left|200px]]
 
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==High resolution structure of ClpN==
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The line below this paragraph, containing "STRUCTURE_1r6c", creates the "Structure Box" on the page.
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<StructureSection load='1r6c' size='340' side='right'caption='[[1r6c]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1r6c]] is a 1 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=1R6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R6C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.15&#8491;</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=1r6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6c OCA], [https://pdbe.org/1r6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6c RCSB], [https://www.ebi.ac.uk/pdbsum/1r6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6c ProSAT]</span></td></tr>
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{{STRUCTURE_1r6c| PDB=1r6c | SCENE= }}
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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/r6/1r6c_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=1r6c ConSurf].
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<div style="clear:both"></div>
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'''High resolution structure of ClpN'''
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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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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.
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==About this Structure==
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1R6C is a [[Single protein]] structure of sequence 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=1R6C OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15037248 15037248]
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[[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: 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: Aaa+]]
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[[Category: Binding mechanism]]
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[[Category: Clpa]]
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[[Category: Clp]]
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[[Category: Crystal]]
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[[Category: N-terminal domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:08:13 2008''
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Current revision

High resolution structure of ClpN

PDB ID 1r6c

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