2p32
From Proteopedia
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|PDB= 2p32 |SIZE=350|CAPTION= <scene name='initialview01'>2p32</scene>, resolution 3.200Å | |PDB= 2p32 |SIZE=350|CAPTION= <scene name='initialview01'>2p32</scene>, resolution 3.200Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= hsp-1, hsp70a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]) | |GENE= hsp-1, hsp70a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p32 OCA], [http://www.ebi.ac.uk/pdbsum/2p32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p32 RCSB]</span> | ||
}} | }} | ||
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[[Category: Walkinshaw, M D.]] | [[Category: Walkinshaw, M D.]] | ||
[[Category: Worrall, L J.]] | [[Category: Worrall, L J.]] | ||
| - | [[Category: SO4]] | ||
[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:28:05 2008'' |
Revision as of 01:28, 31 March 2008
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| , resolution 3.200Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | hsp-1, hsp70a (Caenorhabditis elegans) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70
Overview
Hsp70 chaperones are composed of two domains; the 40 kDa N-terminal nucleotide-binding domain (NDB) and the 30 kDa 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 18 kDa beta-sandwich subdomain, which forms the hydrophobic binding pocket, and a 10 kDa 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 10 kDa 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.
About this Structure
2P32 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70., Worrall LJ, Walkinshaw MD, Biochem Biophys Res Commun. 2007 May 25;357(1):105-10. Epub 2007 Mar 28. PMID:17407764
Page seeded by OCA on Mon Mar 31 04:28:05 2008
