1qlg: Difference between revisions

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New page: left|200px<br /> <applet load="1qlg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qlg, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF...
 
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==About this Structure==
==About this Structure==
1QLG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]] with CA and MG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QLG OCA]].  
1QLG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]] with CA and MG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: MG. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QLG OCA]].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10655618 10655618]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10655618 10655618]
[[Category: 3-phytase]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thermostable]]
[[Category: thermostable]]


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Revision as of 14:17, 30 October 2007

File:1qlg.gif


1qlg, resolution 2.2Å

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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 ... [(full description)]

About this StructureAbout this Structure

1QLG is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA and MG as [ligands]. Active as [3-phytase], with EC number [3.1.3.8]. Structure known Active Site: MG. 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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