1asx
From Proteopedia
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|PDB= 1asx |SIZE=350|CAPTION= <scene name='initialview01'>1asx</scene>, resolution 2.8Å | |PDB= 1asx |SIZE=350|CAPTION= <scene name='initialview01'>1asx</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= THSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | |GENE= THSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1asx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asx OCA], [http://www.ebi.ac.uk/pdbsum/1asx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1asx RCSB]</span> | ||
}} | }} | ||
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[[Category: Essen, L O.]] | [[Category: Essen, L O.]] | ||
[[Category: Klumpp, M.]] | [[Category: Klumpp, M.]] | ||
| - | [[Category: PO4]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
[[Category: chaperonin]] | [[Category: chaperonin]] | ||
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[[Category: thermosome]] | [[Category: thermosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:46:58 2008'' |
Revision as of 15:46, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | THSA (Thermoplasma acidophilum) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM
Overview
The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution. The core resembles the apical domain of GroEL but lacks the hydrophobic residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix motif, which is characteristic of all group II chaperonins including the eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are consistent with cryo electron microscopy data, suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaperonin.
About this Structure
1ASX is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin., Klumpp M, Baumeister W, Essen LO, Cell. 1997 Oct 17;91(2):263-70. PMID:9346243
Page seeded by OCA on Sun Mar 30 18:46:58 2008
Categories: Single protein | Thermoplasma acidophilum | Baumeister, W. | Essen, L O. | Klumpp, M. | Atp-binding | Chaperonin | Groel | Hsp60 | Tcp1 | Thermosome
