1dkl: Difference between revisions

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[[Image:1dkl.gif|left|200px]]
[[Image:1dkl.gif|left|200px]]


{{Structure
<!--
|PDB= 1dkl |SIZE=350|CAPTION= <scene name='initialview01'>1dkl</scene>, resolution 2.30&Aring;
The line below this paragraph, containing "STRUCTURE_1dkl", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE=
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|DOMAIN=
{{STRUCTURE_1dkl| PDB=1dkl | SCENE= }}  
|RELATEDENTRY=[[1dkl|1DKL]], [[1dkm|1DKM]], [[1dkn|1DKN]], [[1dko|1DKO]], [[1dkp|1DKP]], [[1dkq|1DKQ]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkl OCA], [http://www.ebi.ac.uk/pdbsum/1dkl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dkl RCSB]</span>
}}


'''CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 4.5 (NO LIGAND BOUND)'''
'''CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 4.5 (NO LIGAND BOUND)'''
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[[Category: Jia, Z.]]
[[Category: Jia, Z.]]
[[Category: Lim, D.]]
[[Category: Lim, D.]]
[[Category: histidine acid phosphatase fold]]
[[Category: Histidine acid phosphatase fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:57:27 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:22 2008''

Revision as of 13:57, 2 May 2008

File:1dkl.gif

Template:STRUCTURE 1dkl

CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 4.5 (NO LIGAND BOUND)


OverviewOverview

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.

About this StructureAbout this Structure

1DKL 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 Fri May 2 13:57:27 2008

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