1rpt
From Proteopedia
(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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| - | [[Image:1rpt.gif|left|200px]]<br /><applet load="1rpt" size=" | + | [[Image:1rpt.gif|left|200px]]<br /><applet load="1rpt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rpt, resolution 3.0Å" /> | caption="1rpt, resolution 3.0Å" /> | ||
'''CRYSTAL STRUCTURES OF RAT ACID PHOSPHATASE COMPLEXED WITH THE TRANSITIONS STATE ANALOGS VANADATE AND MOLYBDATE: IMPLICATIONS FOR THE REACTION MECHANISM'''<br /> | '''CRYSTAL STRUCTURES OF RAT ACID PHOSPHATASE COMPLEXED WITH THE TRANSITIONS STATE ANALOGS VANADATE AND MOLYBDATE: IMPLICATIONS FOR THE REACTION MECHANISM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structures of complexes of recombinant rat prostatic | + | 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== | ==About this Structure== | ||
| - | 1RPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAG and VO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http:// | + | 1RPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=VO4:'>VO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase(phosphoric monoester)]] | [[Category: hydrolase(phosphoric monoester)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:18 2008'' |
Revision as of 12:53, 21 February 2008
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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 and 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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