3F41

Structure of the tandemly repeated protein tyrosine phosphatase like phytase from Mitsuokella multacida

Summary for 3F41

• Entry DOI: 10.2210/pdb3f41/pdb
• Related: 2PSZ
• Descriptor: Phytase, PHOSPHATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: phytase, tandem repeat, protein tyrosine phosphatase, inositol phosphatase, hydrolase
• Biological source: Mitsuokella multacida
• Total number of polymer chains: 2
• Total formula weight: 145296.11

Authors

Gruninger, R.J.,Selinger, L.B.,Mosimann, S.C. (deposition date: 2008-10-31, release date: 2009-06-09, Last modification date: 2023-12-27)

Primary citation

Gruninger, R.J.,Selinger, L.B.,Mosimann, S.C.
Structural analysis of a multifunctional, tandemly repeated inositol polyphosphatase.
J.Mol.Biol., 392:75-86, 2009

PubMed Abstract: Mitsuokella multacida expresses a unique inositol polyphosphatase (PhyAmm) that is composed of tandem repeats (TRs). Each repeat possesses a protein tyrosine phosphatase (PTP) active-site signature sequence and fold. Using a combination of structural, mutational, and kinetic studies, we show that the N-terminal (D1) and C-terminal (D2) active sites of the TR have diverged and possess significantly different specificities for inositol polyphosphate. Structural analysis and molecular docking calculations identify steric and electrostatic differences within the substrate binding pocket of each TR that may be involved in the altered substrate specificity. The implications of our results for the biological function of related PTP-like phytases are discussed. Finally, the structures and activities of PhyAmm and tandemly repeated receptor PTPs are compared and discussed. To our knowledge, this is the first example of an inositol phosphatase with tandem PTP domains possessing substrate specificity for different inositol phosphates.

PubMed: 19500593
DOI: 10.1016/j.jmb.2009.05.079

Experimental method

X-RAY DIFFRACTION (2.3 Å)