2b4u: Difference between revisions
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|PDB= 2b4u |SIZE=350|CAPTION= <scene name='initialview01'>2b4u</scene>, resolution 2.000Å | |PDB= 2b4u |SIZE=350|CAPTION= <scene name='initialview01'>2b4u</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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_C252S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 Selenomonas ruminantium]) | |GENE= phyasr_C252S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=971 Selenomonas ruminantium]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2b4o|2B4O]], [[2b4p|2B4P]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4u OCA], [http://www.ebi.ac.uk/pdbsum/2b4u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b4u RCSB]</span> | |||
}} | }} | ||
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[[Category: Mosimann, S C.]] | [[Category: Mosimann, S C.]] | ||
[[Category: Selinger, L B.]] | [[Category: Selinger, L B.]] | ||
[[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 02:01:32 2008'' | ||
Revision as of 02:01, 31 March 2008
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| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | phyasr_C252S (Selenomonas ruminantium) | ||||||
| Activity: | 5-phytase, with EC number 3.1.3.72 | ||||||
| Related: | 2B4O, 2B4P
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the C252S mutant of Selenomonas ruminantium PTP-like phytase
OverviewOverview
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 StructureAbout this Structure
2B4U is a Single protein structure of sequence from Selenomonas ruminantium. Full crystallographic information is available from OCA.
ReferenceReference
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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