2NZO

Crystal structure of a secretion chaperone CsaA from Bacillus subtilis in the space group P 32 2 1

2NZO の概要

• エントリーDOI: 10.2210/pdb2nzo/pdb
• 関連するPDBエントリー: 2NZH
• 分子名称: Protein csaA, GLYCEROL (3 entities in total)
• 機能のキーワード: beta barrel, oligonucleotide/oligosaccharide binding fold, ob fold, homodimer, chaperone
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm (Probable): P37584
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49365.15

構造登録者

Shapova, Y.A.,Paetzel, M. (登録日: 2006-11-24, 公開日: 2007-03-27, 最終更新日: 2023-08-30)

主引用文献

Shapova, Y.A.,Paetzel, M.
Crystallographic analysis of Bacillus subtilis CsaA.
Acta Crystallogr.,Sect.D, 63:478-485, 2007

PubMed Abstract: Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups (P42(1)2 and P3(2)21) solved and refined to resolutions of 1.9 and 2.0 A, respectively. These structures complement the previously available crystal structure of CsaA from the Gram-negative eubacterium Thermus thermophilus (TtCsaA) and provide a direct structural basis for the interpretation of previously available biochemical data on BsCsaA. The sequence and structure of the proposed substrate-binding pocket are analyzed and discussed. A comparison with the TtCsaA structure reveals a different pattern of electrostatic potential in the vicinity of the binding site, which overlaps with a region of high sequence variability. In addition, the dimerization interface of this homodimeric protein is analyzed and discussed.

PubMed: 17372352
DOI: 10.1107/S0907444907005045

実験手法

X-RAY DIFFRACTION (2 Å)