1dko: Difference between revisions

Revision as of 23:13, 30 June 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:1dko.png

Template:STRUCTURE 1dko

CRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGECRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE

Template:ABSTRACT PUBMED 10655611

About this StructureAbout this Structure

1DKO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of Escherichia coli phytase and its complex with phytate., Lim D, Golovan S, Forsberg CW, Jia Z, Nat Struct Biol. 2000 Feb;7(2):108-13. PMID:10655611

Page seeded by OCA on Mon Jun 30 23:13:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1dko.gif|left|200px]]
+{{Seed}}
+[[Image:1dko.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dko|  PDB=1dko  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE'''
+===CRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE===
-==Overview==
+<!--
-Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of E. coli phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of E. coli phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.
+The line below this paragraph, {{ABSTRACT_PUBMED_10655611}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10655611 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10655611}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Lim, D.]]
 [[Category: Histidine acid phosphatase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:57:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:13:03 2008''