1gd7
From Proteopedia
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'''CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.''' | '''CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.''' | ||
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[[Category: Vassylyev, D G.]] | [[Category: Vassylyev, D G.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: Functional dimer]] |
| - | [[Category: | + | [[Category: Hydrophobic cavity]] |
| - | [[Category: | + | [[Category: Oligonucleotide-binding fold]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
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Revision as of 14:26, 2 May 2008
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 Page seeded by OCA on Fri May 2 17:26:15 2008
Categories: Single protein | Thermus thermophilus | Inoue, Y. | Kawaguchi, S. | Kuramitsu, S. | Linde, D. | Muller, J. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shibata, T. | Vassylyev, D G. | Yokoyama, S. | Functional dimer | Hydrophobic cavity | Oligonucleotide-binding fold | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
