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[[Image:2p32.gif|left|200px]]<br /><applet load="2p32" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2p32, resolution 3.200&Aring;" />
'''Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70'''<br />


==Overview==
==Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70==
Hsp70 chaperones are composed of two domains; the 40kDa N-terminal, nucleotide-binding domain (NDB) and the 30kDa C-terminal substrate-binding, domain (SBD). Structures of the SBD from Escherichia coli homologues DnaK, and HscA show it can be further divided into an 18kDa beta-sandwich, subdomain, which forms the hydrophobic binding pocket, and a 10kDa, C-terminal three-helix bundle that forms a lid over the binding pocket., Across prokaryotes and eukaryotes, the NBD and beta-sandwich subdomain are, well conserved in both sequence and structure. The C-terminal subdomain, is, however, more evolutionary variable and the only eukaryotic structure, from rat Hsc70 revealed a diverged helix-loop-helix fold. We have solved, the crystal structure of the C-terminal 10kDa subdomain from, Caenorhabditis elegans Hsp70 which forms a helical-bundle similar to the, prokaryotic homologues. This provides the first confirmation of the, structural conservation of this subdomain in eukaryotes. Comparison with, the rat structure reveals a domain-swap dimerisation mechanism; however, the C. elegans subdomain exists exclusively as a monomer in solution in, agreement with the hypothesis that regions out with the C-terminal, subdomain are necessary for Hsp70 self-association.
<StructureSection load='2p32' size='340' side='right'caption='[[2p32]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2p32]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P32 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p32 OCA], [https://pdbe.org/2p32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p32 RCSB], [https://www.ebi.ac.uk/pdbsum/2p32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p32 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSP1_CAEEL HSP1_CAEEL]
== 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/p3/2p32_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=2p32 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2P32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P32 OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70., Worrall LJ, Walkinshaw MD, Biochem Biophys Res Commun. 2007 Mar 28;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17407764 17407764]
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Walkinshaw, M.D.]]
[[Category: Walkinshaw MD]]
[[Category: Worrall, L.J.]]
[[Category: Worrall LJ]]
[[Category: SO4]]
[[Category: three-helix bundle]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:19:51 2008''

Latest revision as of 12:07, 21 February 2024

Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70

Structural highlights

2p32 is a 6 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSP1_CAEEL

Evolutionary Conservation

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

See Also

2p32, resolution 3.20Å

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