Format

Send to

Choose Destination
See comment in PubMed Commons below
J Mol Biol. 2011 Oct 14;413(1):24-31. doi: 10.1016/j.jmb.2011.08.015. Epub 2011 Aug 17.

Structure and substrate recognition of the Staphylococcus aureus protein tyrosine phosphatase PtpA.

Author information

1
Seattle Biomedical Research Institute, Seattle, WA 98109, USA.

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.

PMID:
21871460
PMCID:
PMC3204379
DOI:
10.1016/j.jmb.2011.08.015
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center