2b4p
From Proteopedia
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| - | [[Image:2b4p.jpg|left|200px]] | + | [[Image:2b4p.jpg|left|200px]] |
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| - | '''Structure of the D223N mutant of Selenomonas ruminantium PTP-like phytase''' | + | {{Structure |
| + | |PDB= 2b4p |SIZE=350|CAPTION= <scene name='initialview01'>2b4p</scene>, resolution 1.81Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=MLI:MALONATE ION'>MLI</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/5-phytase 5-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.72 3.1.3.72] | ||
| + | |GENE= phyasr_R252K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 Selenomonas ruminantium]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of the D223N mutant of Selenomonas ruminantium PTP-like phytase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2B4P is a [ | + | 2B4P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Selenomonas_ruminantium Selenomonas ruminantium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4P OCA]. |
==Reference== | ==Reference== | ||
| - | Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase., Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB, Protein Sci. 2007 Jul;16(7):1368-78. Epub 2007 Jun 13. PMID:[http:// | + | Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase., Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB, Protein Sci. 2007 Jul;16(7):1368-78. Epub 2007 Jun 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17567745 17567745] |
[[Category: 5-phytase]] | [[Category: 5-phytase]] | ||
[[Category: Selenomonas ruminantium]] | [[Category: Selenomonas ruminantium]] | ||
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[[Category: ptp-like]] | [[Category: ptp-like]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:35 2008'' |
Revision as of 13:57, 20 March 2008
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| , resolution 1.81Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | phyasr_R252K (Selenomonas ruminantium) | ||||||
| Activity: | 5-phytase, with EC number 3.1.3.72 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the D223N mutant of Selenomonas ruminantium PTP-like phytase
Overview
PhyA from Selenomonas ruminantium (PhyAsr), is a bacterial protein tyrosine phosphatase (PTP)-like inositol polyphosphate phosphatase (IPPase) that is distantly related to known PTPs. PhyAsr has a second substrate binding site referred to as a standby site and the P-loop (HCX5R) has been observed in both open (inactive) and closed (active) conformations. Site-directed mutagenesis and kinetic and structural studies indicate PhyAsr follows a classical PTP mechanism of hydrolysis and has a broad specificity toward polyphosphorylated myo-inositol substrates, including phosphoinositides. Kinetic and molecular docking experiments demonstrate PhyAsr preferentially cleaves the 3-phosphate position of Ins P6 and will produce Ins(2)P via a highly ordered series of sequential dephosphorylations: D-Ins(1,2,4,5,6)P5, Ins(2,4,5,6)P4, D-Ins(2,4,5)P3, and D-Ins(2,4)P2. The data support a distributive enzyme mechanism and suggest the PhyAsr standby site is involved in the recruitment of substrate. Structural studies at physiological pH and high salt concentrations demonstrate the "closed" or active P-loop conformation can be induced in the absence of substrate. These results suggest PhyAsr should be reclassified as a D-3 myo-inositol hexakisphosphate phosphohydrolase and suggest the PhyAsr reaction mechanism is more similar to that of PTPs than previously suspected.
About this Structure
2B4P is a Single protein structure of sequence from Selenomonas ruminantium. Full crystallographic information is available from OCA.
Reference
Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase., Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB, Protein Sci. 2007 Jul;16(7):1368-78. Epub 2007 Jun 13. PMID:17567745
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