1ywf

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spinqualitylabelsall models 1ywf, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Mycobacterium Tuberculosis Protein Tyrosine Phosphatase PtpB

Overview

Intracellular pathogenic bacteria manipulate host signal transduction, pathways to facilitate infection. Mycobacterium tuberculosis protein, tyrosine phosphatases (PTPs) PtpA and PtpB are thought to be secreted into, host cells and interfere with unidentified signals. To illuminate the, mechanisms of regulation and substrate recognition, we determined the 1.7, A resolution crystal structure of PtpB in complex with the product, phosphate. The protein adopts a simplified PTP fold, which combines, features of the conventional PTPs and dual-specificity phosphatases. PtpB, shows two unusual elaborations--a disordered, acidic loop and a flexible, two-helix lid that covers the active site--that are specific to, mycobacterial orthologs. Biochemical studies suggest that substrate, mimicry in the lid may protect the phosphatase from oxidative, inactivation. The insertion and deletion of large structural elements in, PtpB suggest that, outside the active site module, the PTP family is under, unusual selective pressure that promotes changes in overall structure.

About this Structure

1YWF is a Single protein structure of sequence from Mycobacterium tuberculosis with PO4 as ligand. Full crystallographic information is available from OCA.

Reference

Mycobacterium tuberculosis protein tyrosine phosphatase PtpB structure reveals a diverged fold and a buried active site., Grundner C, Ng HL, Alber T, Structure. 2005 Nov;13(11):1625-34. PMID:16271885

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