2b82: Difference between revisions

Revision as of 23:28, 27 July 2008

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File:2b82.png

Template:STRUCTURE 2b82

Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolutionCrystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolution

Template:ABSTRACT PUBMED 16330049

About this StructureAbout this Structure

2B82 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1rmw. Full crystallographic information is available from OCA.

ReferenceReference

A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases., Calderone V, Forleo C, Benvenuti M, Thaller MC, Rossolini GM, Mangani S, J Mol Biol. 2006 Jan 27;355(4):708-21. Epub 2005 Nov 10. PMID:16330049

Page seeded by OCA on Sun Jul 27 23:28:45 2008

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OCA

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-'''Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolution'''
+===Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolution===
-==Overview==
+<!--
-The Escherichia coli gene aphA codes for a periplasmic acid phosphatase called AphA, belonging to class B bacterial phosphatases, which is part of the DDDD superfamily of phosphohydrolases. After our first report about its crystal structure, we have started a series of crystallographic studies aimed at understanding of the catalytic mechanism of the enzyme. Here, we report three crystal structures of the AphA enzyme in complex with the hydrolysis products of nucleoside monophosphate substrates and a fourth with a proposed intermediate analogue that appears to be covalently bound to the enzyme. Comparison with the native enzyme structure and with the available X-ray structures of different phosphatases provides clues about the enzyme chemistry and allows us to propose a catalytic mechanism for AphA, and to discuss it with respect to the mechanism of other bacterial and human phosphatases.
+The line below this paragraph, {{ABSTRACT_PUBMED_16330049}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16330049 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16330049}}
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 [[Category: Dddd acid phosphatase]]
 [[Category: Metallo-enzyme]]
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