2b4p
From Proteopedia
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|PDB= 2b4p |SIZE=350|CAPTION= <scene name='initialview01'>2b4p</scene>, resolution 1.81Å | |PDB= 2b4p |SIZE=350|CAPTION= <scene name='initialview01'>2b4p</scene>, resolution 1.81Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= phyasr_R252K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 Selenomonas ruminantium]) | |GENE= phyasr_R252K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 Selenomonas ruminantium]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[iu24|IU24]], [[iu25|IU25]], [[iu26|IU26]], [[2b40|2B40]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4p OCA], [http://www.ebi.ac.uk/pdbsum/2b4p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b4p RCSB]</span> | ||
}} | }} | ||
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[[Category: Mosimann, S C.]] | [[Category: Mosimann, S C.]] | ||
[[Category: Selinger, L B.]] | [[Category: Selinger, L B.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MLI]] | ||
[[Category: ionic strength]] | [[Category: ionic strength]] | ||
[[Category: ptp-like]] | [[Category: ptp-like]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:24 2008'' |
Revision as of 23:01, 30 March 2008
| |||||||
| , resolution 1.81Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | phyasr_R252K (Selenomonas ruminantium) | ||||||
| Activity: | 5-phytase, with EC number 3.1.3.72 | ||||||
| Related: | IU24, IU25, IU26, 2B40
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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