1QGQ

UDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS

1QGQ の概要

• エントリーDOI: 10.2210/pdb1qgq/pdb
• 関連するPDBエントリー: 1QG8 1QGS
• 分子名称: PROTEIN (SPORE COAT POLYSACCHARIDE BIOSYNTHESIS PROTEIN SPSA), MANGANESE (II) ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: glycosyltransferase, transferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30666.43

構造登録者

Charnock, S.J. (登録日: 1999-05-04, 公開日: 2000-05-04, 最終更新日: 2024-10-16)

主引用文献

Charnock, S.J.,Davies, G.J.
Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms.
Biochemistry, 38:6380-6385, 1999

PubMed Abstract: The enzymatic formation of glycosidic bonds may be catalyzed by the transfer of the glycosyl moiety from an activated nucleotide-diphospho-sugar donor to a specific acceptor. SpsA is a glycosyltransferase implicated in the synthesis of the spore coat of Bacillus subtilis, whose homologues include cellulose synthase and many lipopolysaccharide and bacterial O-antigen synthases. The three-dimensional crystal structure of SpsA has been determined by conventional MIR techniques at a resolution of 1.5 A. It is a two-domain protein with a nucleotide-binding domain together with an acceptor binding domain which features a disordered loop spanning the active site. The structures of SpsA in complex with both Mg-UDP and Mn-UDP have also been determined at 2.0 and 1.7 A, respectively. These complexes, together with the sequence conservation, begin to shed light on the mechanism of this ubiquitous family of inverting glycosyltransferases.

PubMed: 10350455
DOI: 10.1021/bi990270y

実験手法

X-RAY DIFFRACTION (1.5 Å)