1gd7

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Revision as of 23:04, 24 November 2007

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spinqualitylabelsall models 1gd7, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.

Overview

The CsaA protein was first characterized in Bacillus subtilis as a, molecular chaperone with export-related activities. Here we report the 2.0, Angstrom-resolution crystal structure of the Thermus thermophilus CsaA, protein, designated ttCsaA. Atomic structure and experiments in solution, revealed a homodimer as the functional unit. The structure of the ttCsaA, monomer is reminiscent of the well known oligonucleotide-binding fold, with the addition of extensions at the N- and C-termini that form an, extensive dimer interface. The two identical, large, hydrophobic cavities, on the protein surface are likely to constitute the substrate binding, sites. The CsaA proteins share essential sequence similarity with the, tRNA-binding protein Trbp111. Structure-based sequence analysis suggests a, close structural resemblance between these proteins, which may extend to, the architecture of the binding sites at the atomic level. These results, raise the intriguing possibility that CsaA proteins possess a second, tRNA-binding activity in addition to their export-related function.

About this Structure

1GD7 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus., Kawaguchi S, Muller J, Linde D, Kuramitsu S, Shibata T, Inoue Y, Vassylyev DG, Yokoyama S, EMBO J. 2001 Feb 1;20(3):562-9. PMID:11157762

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