1dkp: Difference between revisions

Line 1:

[[Image:1dkp.~~jpg~~|left|200px]]

[[Image:1dkp.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~CRYSTAL STRUCTURE OF PHYTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS AS AN INTERMOLECULAR BRIDGE~~'''~~

===CRYSTAL STRUCTURE OF PHYTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS 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.

-->

==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:~~57:47~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:13:05 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1dkp.jpg|left|200px]]
+{{Seed}}
+[[Image:1dkp.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dkp|  PDB=1dkp  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF PHYTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS AS AN INTERMOLECULAR BRIDGE'''
+===CRYSTAL STRUCTURE OF PHYTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS 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 13:57:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:13:05 2008''