3T00

Crystal Structure of Phosphonoacetate hydrolase from Sinorhizobium meliloti 1021 in complex with vanadate

Summary for 3T00

• Entry DOI: 10.2210/pdb3t00/pdb
• Related: 3SZY 3SZZ 3T01 3T02
• Descriptor: phosphonoacetate hydrolase, ZINC ION, VANADATE ION, ... (5 entities in total)
• Functional Keywords: alkaline phosphatase superfamily, transition state mimic, hydrolase
• Biological source: Sinorhizobium meliloti (Ensifer meliloti)
• Total number of polymer chains: 1
• Total formula weight: 46898.32

Authors

Agarwal, V.,Nair, S.K. (deposition date: 2011-07-19, release date: 2011-08-03, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)