This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2b4p

From Proteopedia

Revision as of 13:57, 20 March 2008 by OCA (Talk | contribs)
Jump to: navigation, search


PDB ID 2b4p

Drag the structure with the mouse to rotate
, 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

Page seeded by OCA on Thu Mar 20 15:57:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools