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| {{STRUCTURE_1u24| PDB=1u24 | SCENE= }} | | {{STRUCTURE_1u24| PDB=1u24 | SCENE= }} |
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| '''Crystal structure of Selenomonas ruminantium phytase'''
| | ===Crystal structure of Selenomonas ruminantium phytase=== |
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| ==Overview==
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| Various inositide phosphatases participate in the regulation of inositol polyphosphate signaling molecules. Plant phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and phosphate. The phytase from Selenomonas ruminantium shares no sequence homology with other microbial phytases. Its crystal structure revealed a phytase fold of the dual-specificity phosphatase type. The active site is located near a conserved cysteine-containing (Cys241) P loop. We also solved two other crystal forms in which an inhibitor, myo-inositol hexasulfate, is cocrystallized with the enzyme. In the "standby" and the "inhibited" crystal forms, the inhibitor is bound, respectively, in a pocket slightly away from Cys241 and at the substrate binding site where the phosphate group to be hydrolyzed is held close to the -SH group of Cys241. Our structural and mutagenesis studies allow us to visualize the way in which the P loop-containing phytase attracts and hydrolyzes the substrate (phytate) sequentially.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15530366}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15530366 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15530366}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Phytase]] | | [[Category: Phytase]] |
| [[Category: Ptp]] | | [[Category: Ptp]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:39:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:23:35 2008'' |
