1qlg: Difference between revisions
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|PDB= 1qlg |SIZE=350|CAPTION= <scene name='initialview01'>1qlg</scene>, resolution 2.2Å | |PDB= 1qlg |SIZE=350|CAPTION= <scene name='initialview01'>1qlg</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=MG:Mg'>MG</scene> | |SITE= <scene name='pdbsite=MG:Mg'>MG</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qlg OCA], [http://www.ebi.ac.uk/pdbsum/1qlg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qlg RCSB]</span> | |||
}} | }} | ||
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[[Category: Oh, B H.]] | [[Category: Oh, B H.]] | ||
[[Category: Shin, S.]] | [[Category: Shin, S.]] | ||
[[Category: calcium]] | [[Category: calcium]] | ||
[[Category: magnesium]] | [[Category: magnesium]] | ||
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[[Category: thermostable]] | [[Category: thermostable]] | ||
''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 23:15:26 2008'' | ||
Revision as of 23:15, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | 3-phytase, with EC number 3.1.3.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PHYTASE WITH MAGNESIUM FROM BACILLUS AMYLOLIQUEFACIENS
OverviewOverview
Phytases hydrolyze phytic acid to less phosphorylated myo-inositol derivatives and inorganic phosphate. A thermostable phytase is of great value in applications for improving phosphate and metal ion availability in animal feed, and thereby reducing phosphate pollution to the environment. Here, we report a new folding architecture of a six-bladed propeller for phosphatase activity revealed by the 2.1 A crystal structures of a novel, thermostable phytase determined in both the partially and fully Ca2+-loaded states. Binding of two calcium ions to high-affinity calcium binding sites results in a dramatic increase in thermostability (by as much as approximately 30 degrees C in melting temperature) by joining loop segments remote in the amino acid sequence. Binding of three additional calcium ions to low-affinity calcium binding sites at the top of the molecule turns on the catalytic activity of the enzyme by converting the highly negatively charged cleft into a favorable environment for the binding of phytate.
About this StructureAbout this Structure
1QLG is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states., Ha NC, Oh BC, Shin S, Kim HJ, Oh TK, Kim YO, Choi KY, Oh BH, Nat Struct Biol. 2000 Feb;7(2):147-53. PMID:10655618
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