1rpt
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(New page: 200px<br /><applet load="1rpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpt, resolution 3.0Å" /> '''CRYSTAL STRUCTURES OF...)
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Revision as of 23:39, 20 November 2007
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CRYSTAL STRUCTURES OF RAT ACID PHOSPHATASE COMPLEXED WITH THE TRANSITIONS STATE ANALOGS VANADATE AND MOLYBDATE: IMPLICATIONS FOR THE REACTION MECHANISM
Overview
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.
About this Structure
1RPT is a Single protein structure of sequence from Rattus norvegicus with NAG and VO4 as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.
Reference
Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism., Lindqvist Y, Schneider G, Vihko P, Eur J Biochem. 1994 Apr 1;221(1):139-42. PMID:8168503
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