1GD7

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

Summary for 1GD7

• Entry DOI: 10.2210/pdb1gd7/pdb
• Descriptor: CSAA PROTEIN (2 entities in total)
• Functional Keywords: oligonucleotide-binding fold, functional dimer, hydrophobic cavity, riken structural genomics/proteomics initiative, rsgi, structural genomics, rna binding protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 4
• Total formula weight: 47659.96

Authors

Shibata, T.,Inoue, Y.,Vassylyev, D.G.,Kawaguchi, S.,Yokoyama, S.,Muller, J.,Linde, D.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2000-09-22, release date: 2001-09-22, Last modification date: 2023-12-27)

Primary citation

Kawaguchi, S.,Muller, J.,Linde, D.,Kuramitsu, S.,Shibata, T.,Inoue, Y.,Vassylyev, D.G.,Yokoyama, S.
The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.
EMBO J., 20:562-569, 2001

PubMed Abstract: 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.

PubMed: 11157762
DOI: 10.1093/emboj/20.3.562

Experimental method

X-RAY DIFFRACTION (2 Å)