3ROF

Crystal Structure of the S. aureus Protein Tyrosine Phosphatase PtpA

Summary for 3ROF

• Entry DOI: 10.2210/pdb3rof/pdb
• Descriptor: Low molecular weight protein-tyrosine-phosphatase ptpA, Expression tag cleaved from protein-tyrosine-phosphatase ptpA, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: phosphatase, hydrolase
• Biological source: Staphylococcus aureus; More
• Total number of polymer chains: 2
• Total formula weight: 18989.04

Authors

Grundner, C.,Chou, S.,Engel, K. (deposition date: 2011-04-25, release date: 2011-09-07, Last modification date: 2024-02-28)

Primary citation

Vega, C.,Chou, S.,Engel, K.,Harrell, M.E.,Rajagopal, L.,Grundner, C.
Structure and substrate recognition of the Staphylococcus aureus protein tyrosine phosphatase PtpA.
J.Mol.Biol., 413:24-31, 2011

PubMed Abstract: Phosphosignaling through pSer/pThr/pTyr is emerging as a common signaling mechanism in prokaryotes. The human pathogen Staphylococcus aureus produces two low-molecular-weight protein tyrosine phosphatases (PTPs), PtpA and PtpB, with unknown functions. To provide the structural context for understanding PtpA function and substrate recognition, establish PtpA's structural relations within the PTP family, and provide a framework for the design of specific inhibitors, we solved the crystal structure of PtpA at 1 Å resolution. While PtpA adopts the common, conserved PTP fold and shows close overall similarity to eukaryotic PTPs, several features in the active site and surface organization are unique and can be explored to design selective inhibitors. A peptide bound in the active site mimics a phosphotyrosine substrate, affords insight into substrate recognition, and provides a testable substrate prediction. Genetic deletion of ptpA or ptpB does not affect in vitro growth or cell wall integrity, raising the possibility that PtpA and PtpB have specialized functions during infection.

PubMed: 21871460
DOI: 10.1016/j.jmb.2011.08.015

Experimental method

X-RAY DIFFRACTION (1.03 Å)