3SZY

Crystal Structure of Phosphonoacetate hydrolase from Sinorhizobium meliloti 1021 in APO form

3SZY の概要

• エントリーDOI: 10.2210/pdb3szy/pdb
• 関連するPDBエントリー: 3SZZ 3T00 3T01 3T02
• 分子名称: phosphonoacetate hydrolase, ZINC ION (3 entities in total)
• 機能のキーワード: alkaline phosphatase superfamily, hydrolase
• 由来する生物種: Sinorhizobium meliloti (Ensifer meliloti)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46724.69

構造登録者

Agarwal, V.,Nair, S.K. (登録日: 2011-07-19, 公開日: 2011-08-03, 最終更新日: 2024-02-28)

主引用文献

Agarwal, V.,Borisova, S.A.,Metcalf, W.W.,van der Donk, W.A.,Nair, S.K.
Structural and mechanistic insights into C-p bond hydrolysis by phosphonoacetate hydrolase.
Chem.Biol., 18:1230-1240, 2011

PubMed Abstract: Bacteria have evolved pathways to metabolize phosphonates as a nutrient source for phosphorus. In Sinorhizobium meliloti 1021, 2-aminoethylphosphonate is catabolized to phosphonoacetate, which is converted to acetate and inorganic phosphate by phosphonoacetate hydrolase (PhnA). Here we present detailed biochemical and structural characterization of PhnA that provides insights into the mechanism of C-P bond cleavage. The 1.35 Å resolution crystal structure reveals a catalytic core similar to those of alkaline phosphatases and nucleotide pyrophosphatases but with notable differences, such as a longer metal-metal distance. Detailed structure-guided analysis of active site residues and four additional cocrystal structures with phosphonoacetate substrate, acetate, phosphonoformate inhibitor, and a covalently bound transition state mimic provide insight into active site features that may facilitate cleavage of the C-P bond. These studies expand upon the array of reactions that can be catalyzed by enzymes of the alkaline phosphatase superfamily.

PubMed: 22035792
DOI: 10.1016/j.chembiol.2011.07.019

実験手法

X-RAY DIFFRACTION (1.35 Å)