1r6b: Difference between revisions

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New page: left|200px<br /><applet load="1r6b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6b, resolution 2.25Å" /> '''High resolution crys...
 
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[[Image:1r6b.jpg|left|200px]]<br /><applet load="1r6b" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1r6b, resolution 2.25&Aring;" />
'''High resolution crystal structure of ClpA'''<br />


==Overview==
==High resolution crystal structure of ClpA==
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.
<StructureSection load='1r6b' size='340' side='right'caption='[[1r6b]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1r6b]] 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=1R6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R6B FirstGlance]. <br>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1r6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6b OCA], [https://pdbe.org/1r6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6b RCSB], [https://www.ebi.ac.uk/pdbsum/1r6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6b ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r6/1r6b_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1r6b ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1R6B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R6B OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15037248 15037248]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[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: ADP]]
[[Category: MG]]
[[Category: aaa+]]
[[Category: binding mechanism]]
[[Category: clpa]]
[[Category: clps]]
[[Category: crystal]]
[[Category: n-terminal domain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:18:14 2007''

Latest revision as of 11:20, 14 February 2024

High resolution crystal structure of ClpAHigh resolution crystal structure of ClpA

Structural highlights

1r6b is a 1 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

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.

See Also

1r6b, resolution 2.25Å

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