1RZ2

1.6A crystal structure of the protein BA4783/Q81L49 (similar to sortase B) from Bacillus anthracis.

1RZ2 の概要

• エントリーDOI: 10.2210/pdb1rz2/pdb
• 関連するPDBエントリー: 1NG5
• 分子名称: conserved hypothetical protein BA4783 (2 entities in total)
• 機能のキーワード: sortase b protein, b. anthracis, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30144.94

構造登録者

Wu, R.,Zhang, R.,Gornicki, P.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2003-12-23, 公開日: 2004-07-06, 最終更新日: 2024-02-14)

主引用文献

Zhang, R.,Wu, R.,Joachimiak, G.,Mazmanian, S.K.,Missiakas, D.M.,Gornicki, P.,Schneewind, O.,Joachimiak, A.
Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site.
Structure, 12:1147-1156, 2004

PubMed Abstract: Surface proteins attached by sortases to the cell wall envelope of bacterial pathogens play important roles during infection. Sorting and attachment of these proteins is directed by C-terminal signals. Sortase B of S. aureus recognizes a motif NPQTN, cleaves the polypeptide after the Thr residue, and attaches the protein to pentaglycine cross-bridges. Sortase B of B. anthracis is thought to recognize the NPKTG motif, and attaches surface proteins to m-diaminopimelic acid cross-bridges. We have determined crystal structure of sortase B from B. anthracis and S. aureus at 1.6 and 2.0 A resolutions, respectively. These structures show a beta-barrel fold with alpha-helical elements on its outside, a structure thus far exclusive to the sortase family. A putative active site located on the edge of the beta-barrel is comprised of a Cys-His-Asp catalytic triad and presumably faces the bacterial cell surface. A putative binding site for the sorting signal is located nearby.

PubMed: 15242591
DOI: 10.1016/j.str.2004.06.001

実験手法

X-RAY DIFFRACTION (1.6 Å)