2dxl: Difference between revisions

Revision as of 03:49, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2dxl.png

Template:STRUCTURE 2dxl

Glycerophosphodiesterase from Enterobacter aerogenesGlycerophosphodiesterase from Enterobacter aerogenes

Template:ABSTRACT PUBMED 17306828

About this StructureAbout this Structure

2DXL is a Single protein structure of sequence from Enterobacter aerogenes. Full crystallographic information is available from OCA.

ReferenceReference

The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes., Jackson CJ, Carr PD, Liu JW, Watt SJ, Beck JL, Ollis DL, J Mol Biol. 2007 Apr 6;367(4):1047-62. Epub 2007 Jan 20. PMID:17306828

The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes., Jackson CJ, Carr PD, Kim HK, Liu JW, Ollis DL, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt, 7):659-61. Epub 2006 Jun 10. PMID:16820687

Page seeded by OCA on Tue Jul 29 03:49:12 2008

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OCA

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-[[Image:2dxl.gif|left|200px]]
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 {{STRUCTURE_2dxl|  PDB=2dxl  |  SCENE=  }}
-'''Glycerophosphodiesterase from Enterobacter aerogenes'''
+===Glycerophosphodiesterase from Enterobacter aerogenes===
-==Overview==
+<!--
-The structure of the glycerophosphodiesterase (GDPD) from Enterobacter aerogenes, GpdQ, has been solved by SAD phasing from the active site metal ions. Structural analysis indicates that GpdQ belongs to the alpha/beta sandwich metallo-phosphoesterase family, rather than the (alpha/beta)(8) barrel GDPD family, suggesting that GpdQ is a structurally novel GDPD. Hexameric GpdQ is generated by interactions between three dimers. The dimers are formed through domain swapping, stabilised by an inter-chain disulfide bond, and beta-sheet extension. The active site contains a binuclear metal centre, with a fully occupied alpha-metal ion site, and partially occupied beta-metal ion site, as revealed by anomalous scattering analysis. Using a combination of TLS refinement and normal mode analysis, the dynamic movement of GpdQ was investigated. This analysis suggests that the hexameric quaternary structure stabilises the base of the dimer, which promotes "breathing" of the active site cleft. Comparison with other metallo-phosphodiesterases shows that although the central, catalytic, domain is highly conserved, many of these enzymes possess structurally unrelated secondary domains located at the entrance of the active site. We suggest that this could be a common structural feature of metallo-phosphodiesterases that constrains substrate specificity, preventing non-specific phosphodiester hydrolysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_17306828}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17306828 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17306828}}
 ==About this Structure==
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 ==Reference==
 The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes., Jackson CJ, Carr PD, Liu JW, Watt SJ, Beck JL, Ollis DL, J Mol Biol. 2007 Apr 6;367(4):1047-62. Epub 2007 Jan 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17306828 17306828]
+The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes., Jackson CJ, Carr PD, Kim HK, Liu JW, Ollis DL, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt, 7):659-61. Epub 2006 Jun 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16820687 16820687]
 [[Category: Enterobacter aerogenes]]
 [[Category: Glycerophosphodiester phosphodiesterase]]
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 [[Category: Domain-swapping]]
 [[Category: Metalloenzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:34:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:49:12 2008''