2b82: Difference between revisions

Revision as of 17:35, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

2B82 is a Single protein structure of sequence from Escherichia coli with , and as ligands. This structure supersedes the now removed PDB entry 1RMW. Active as Acid phosphatase, with EC number 3.1.3.2 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

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OCA

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-[[Image:2b82.gif|left|200px]]<br /><applet load="2b82" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2b82.gif|left|200px]]<br /><applet load="2b82" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2b82, resolution 1.25&Aring;" />
 '''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'''<br />
 ==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 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.
 ==About this Structure==
-B82 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, PO4 and ADN as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1RMW. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B82 OCA].
+B82 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=ADN:'>ADN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1RMW. 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=2B82 OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: Forleo, C.]]
 [[Category: Mangani, S.]]
-[[Category: Rossolini, G.M.]]
+[[Category: Rossolini, G M.]]
-[[Category: Thaller, M.C.]]
+[[Category: Thaller, M C.]]
 [[Category: ADN]]
 [[Category: MG]]
@@ Line 25: / Line 25: @@
 [[Category: class b acid phosphatase; dddd acid phosphatase; metallo-enzyme; amp]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:38:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:06 2008''