3L8H

Crystal Structure of D,D-heptose 1.7-bisphosphate phosphatase from B. bronchiseptica complexed with magnesium and phosphate

3L8H の概要

• エントリーDOI: 10.2210/pdb3l8h/pdb
• 関連するPDBエントリー: 3L8E 3L8F 3L8G
• 分子名称: Putative haloacid dehalogenase-like hydrolase, MAGNESIUM ION, ZINC ION, ... (8 entities in total)
• 機能のキーワード: had superfamily, gmhb, d-glycero-d-manno-heptose-1, 7-bisphosphate phosphatase, hydrolase
• 由来する生物種: Bordetella bronchiseptica (Alcaligenes bronchisepticus)
• 細胞内の位置: Cytoplasm : Q7WG29
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78370.01

構造登録者

Nguyen, H.,Peisach, E.,Allen, K.N. (登録日: 2009-12-31, 公開日: 2010-02-02, 最終更新日: 2024-10-30)

主引用文献

Nguyen, H.H.,Wang, L.,Huang, H.,Peisach, E.,Dunaway-Mariano, D.,Allen, K.N.
Structural Determinants of Substrate Recognition in the HAD Superfamily Member d-glycero-d-manno-Heptose-1,7-bisphosphate Phosphatase (GmhB) .
Biochemistry, 49:1082-1092, 2010

PubMed Abstract: The haloalkanoic acid dehalogenase (HAD) enzyme superfamily is the largest family of phosphohydrolases. In HAD members, the structural elements that provide the binding interactions that support substrate specificity are separated from those that orchestrate catalysis. For most HAD phosphatases, a cap domain functions in substrate recognition. However, for the HAD phosphatases that lack a cap domain, an alternate strategy for substrate selection must be operative. One such HAD phosphatase, GmhB of the HisB subfamily, was selected for structure-function analysis. Herein, the X-ray crystallographic structures of Escherichia coli GmhB in the apo form (1.6 A resolution), in a complex with Mg(2+) and orthophosphate (1.8 A resolution), and in a complex with Mg(2+) and d-glycero-d-manno-heptose 1beta,7-bisphosphate (2.2 A resolution) were determined, in addition to the structure of Bordetella bronchiseptica GmhB bound to Mg(2+) and orthophosphate (1.7 A resolution). The structures show that in place of a cap domain, the GmhB catalytic site is elaborated by three peptide inserts or loops that pack to form a concave, semicircular surface around the substrate leaving group. Structure-guided kinetic analysis of site-directed mutants was conducted in parallel with a bioinformatics study of sequence diversification within the HisB subfamily to identify loop residues that serve as substrate recognition elements and that distinguish GmhB from its subfamily counterpart, the histidinol-phosphate phosphatase domain of HisB. We show that GmhB and the histidinol-phosphate phosphatase domain use the same design of three substrate recognition loops inserted into the cap domain yet, through selective residue usage on the loops, have achieved unique substrate specificity and thus novel biochemical function.

PubMed: 20050614
DOI: 10.1021/bi902019q

実験手法

X-RAY DIFFRACTION (1.68 Å)