1RPT

CRYSTAL STRUCTURES OF RAT ACID PHOSPHATASE COMPLEXED WITH THE TRANSITIONS STATE ANALOGS VANADATE AND MOLYBDATE: IMPLICATIONS FOR THE REACTION MECHANISM

Summary for 1RPT

• Entry DOI: 10.2210/pdb1rpt/pdb
• Descriptor: PROSTATIC ACID PHOSPHATASE, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: hydrolase(phosphoric monoester)
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 40613.90

Authors

Lindqvist, Y.,Schneider, G. (deposition date: 1993-11-29, release date: 1994-05-31, Last modification date: 2024-10-16)

Primary citation

Lindqvist, Y.,Schneider, G.,Vihko, P.
Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
Eur.J.Biochem., 221:139-142, 1994

PubMed Abstract: The three-dimensional structures of complexes of recombinant rat prostatic acid phosphatase with the transition-state analogs vanadate and molybdate were determined to 0.3-nm resolution using protein crystallographic methods. The overall structure of the enzyme remains unchanged upon binding of the metal oxyanions; only local conformational differences in the positions of some side chains at the active site were found. The metal oxyanions bind in an identical fashion at the active site with trigonal bipyramidal coordination geometry. The metal ion is within coordination distance of the His12 side chain which is located at one of the axial positions. The three equatorial oxygen atoms interact with the conserved residues Arg11, Arg15, Arg79 and His257. Within hydrogen-bonding distance of the axial oxygen atom is the side chain of the conserved residue Asp258. The implications of these results for the catalytic mechanism of acid phosphatase are discussed.

PubMed: 8168503
DOI: 10.1111/j.1432-1033.1994.tb18722.x

Experimental method

X-RAY DIFFRACTION (3 Å)