2b4o: Difference between revisions

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{{STRUCTURE_2b4o|  PDB=2b4o  |  SCENE=  }}  
{{STRUCTURE_2b4o|  PDB=2b4o  |  SCENE=  }}  


'''Structure of the R258K mutant of Selenomonas ruminantium PTP-like phytase'''
===Structure of the R258K mutant of Selenomonas ruminantium PTP-like phytase===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17567745}}


==About this Structure==
==About this Structure==
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[[Category: Ionic strength]]
[[Category: Ionic strength]]
[[Category: Ptp-like]]
[[Category: Ptp-like]]
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