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1e0r

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0r OCA], [http://www.ebi.ac.uk/pdbsum/1e0r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e0r RCSB]</span>
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[[Category: thermosome]]
[[Category: thermosome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:46 2008''

Revision as of 16:52, 30 March 2008

Image:1e0r.jpg


PDB ID 1e0r

Drag the structure with the mouse to rotate
, resolution 2.8Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



BETA-APICAL DOMAIN OF THERMOSOME


Overview

The crystal structure of the beta-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 A resolution. The structure shows an invariant globular core from which a 25 A long protrusion emanates, composed of an elongated alpha-helix (H10) and a long extended stretch consisting of residues GluB245-ThrB253. A comparison with previous apical domain structures reveals a large segmental displacement of the protruding part of helix H10 via the hinge GluB276-ValB278. The region comprising residues GluB245-ThrB253 adopts an extended beta-like conformation rather than the alpha-helix seen in the alpha-apical domain. Consequently, it appears that the protrusions of the apical domains from group II chaperonins might assume a variety of context-dependent conformations during an open, substrate-accepting state of the chaperonin. Sequence variations in the protrusion regions that are found in the eukaryotic TRiC/CCT subunits may provide different structural propensities and hence serve different roles in substrate recognition.

About this Structure

1E0R is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.

Reference

Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region., Bosch G, Baumeister W, Essen LO, J Mol Biol. 2000 Aug 4;301(1):19-25. PMID:10926489

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