2qxl
From Proteopedia
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|PDB= 2qxl |SIZE=350|CAPTION= <scene name='initialview01'>2qxl</scene>, resolution 2.410Å | |PDB= 2qxl |SIZE=350|CAPTION= <scene name='initialview01'>2qxl</scene>, resolution 2.410Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SSE1, MSI3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= SSE1, MSI3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qxl OCA], [http://www.ebi.ac.uk/pdbsum/2qxl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qxl RCSB]</span> | ||
}} | }} | ||
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[[Category: Hendrickson, W A.]] | [[Category: Hendrickson, W A.]] | ||
[[Category: Liu, Q.]] | [[Category: Liu, Q.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: K]] | ||
| - | [[Category: MG]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: atp state]] | [[Category: atp state]] | ||
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[[Category: stress response]] | [[Category: stress response]] | ||
| - | ''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 04:54:28 2008'' |
Revision as of 01:54, 31 March 2008
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| , resolution 2.410Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | SSE1, MSI3 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of Sse1, a yeast Hsp110
Overview
Classic Hsp70 chaperones assist in diverse processes of protein folding and translocation, and Hsp110s had seemed by sequence to be distant relatives within an Hsp70 superfamily. The 2.4 A resolution structure of Sse1 with ATP shows that Hsp110s are indeed Hsp70 relatives, and it provides insight into allosteric coupling between sites for ATP and polypeptide-substrate binding in Hsp70s. Subdomain structures are similar in intact Sse1(ATP) and in the separate Hsp70 domains, but conformational dispositions are radically different. Interfaces between Sse1 domains are extensive, intimate, and conservative in sequence with Hsp70s. We propose that Sse1(ATP) may be an evolutionary vestige of the Hsp70(ATP) state, and an analysis of 64 mutant variants in Sse1 and three Hsp70 homologs supports this hypothesis. An atomic-level understanding of Hsp70 communication between ATP and substrate-binding domains follows. Requirements on Sse1 for yeast viability are in keeping with the distinct function of Hsp110s as nucleotide exchange factors.
About this Structure
2QXL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Insights into hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1., Liu Q, Hendrickson WA, Cell. 2007 Oct 5;131(1):106-20. PMID:17923091
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