1dkm
From Proteopedia
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|PDB= 1dkm |SIZE=350|CAPTION= <scene name='initialview01'>1dkm</scene>, resolution 2.25Å | |PDB= 1dkm |SIZE=350|CAPTION= <scene name='initialview01'>1dkm</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dkl|1DKL]], [[1dkn|1DKN]], [[1dko|1DKO]], [[1dkp|1DKP]], [[1dkq|1DKQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkm OCA], [http://www.ebi.ac.uk/pdbsum/1dkm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dkm RCSB]</span> | ||
}} | }} | ||
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[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
[[Category: Lim, D.]] | [[Category: Lim, D.]] | ||
| - | [[Category: HG]] | ||
[[Category: histidine acid phosphatase fold]] | [[Category: histidine acid phosphatase fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:25 2008'' |
Revision as of 16:43, 30 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Related: | 1DKL, 1DKN, 1DKO, 1DKP, 1DKQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ESCHERICHIA COLI PHYTASE AT PH 6.6 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.
About this Structure
1DKM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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