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

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Vega C,Chou S,Engel K,Harrell ME,Rajagopal L,Grundner C

doi

10.1016/j.jmb.2011.08.015

subject

Has Abstract

pub_date

2011-10-14 00:00:00

pages

24-31

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(11)00897-7

journal_volume

413

pub_type

杂志文章

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