1ksf: Difference between revisions

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[[Image:1ksf.gif|left|200px]]


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==Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains==
The line below this paragraph, containing "STRUCTURE_1ksf", creates the "Structure Box" on the page.
<StructureSection load='1ksf' size='340' side='right'caption='[[1ksf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ksf]] 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=1KSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KSF FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<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=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
{{STRUCTURE_1ksf| PDB=1ksf |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ksf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksf OCA], [https://pdbe.org/1ksf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ksf RCSB], [https://www.ebi.ac.uk/pdbsum/1ksf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksf 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/ks/1ksf_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=1ksf ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains'''
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Overview==
</StructureSection>
Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity.
 
==About this Structure==
1KSF 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=1KSF OCA].
 
==Reference==
Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease., Guo F, Maurizi MR, Esser L, Xia D, J Biol Chem. 2002 Nov 29;277(48):46743-52. Epub 2002 Aug 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12205096 12205096]
[[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: Xia, D.]]
[[Category: Xia D]]
[[Category: Aaa+]]
[[Category: Atp-dependent protease]]
[[Category: Atpase]]
[[Category: Chaperone]]
[[Category: Clpa]]
[[Category: Crystal structure]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:06:54 2008''

Latest revision as of 10:27, 14 February 2024

Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domainsCrystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains

Structural highlights

1ksf 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 2.6Å
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

1ksf, resolution 2.60Å

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