1GD7

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

1GD7 の概要

• エントリーDOI: 10.2210/pdb1gd7/pdb
• 分子名称: CSAA PROTEIN (2 entities in total)
• 機能のキーワード: oligonucleotide-binding fold, functional dimer, hydrophobic cavity, riken structural genomics/proteomics initiative, rsgi, structural genomics, rna binding protein
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 47659.96

構造登録者

Shibata, T.,Inoue, Y.,Vassylyev, D.G.,Kawaguchi, S.,Yokoyama, S.,Muller, J.,Linde, D.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2000-09-22, 公開日: 2001-09-22, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)