1txo

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spinqualitylabelsall models 1txo, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.

Overview

Serine/threonine protein phosphatases are central mediators of, phosphorylation-dependent signals in eukaryotes and a variety of, pathogenic bacteria. Here, we report the crystal structure of the, intracellular catalytic domain of Mycobacterium tuberculosis PstPpp, a, membrane-anchored phosphatase in the PP2C family. Despite sharing the fold, and two-metal center of human PP2Calpha, the PstPpp catalytic domain binds, a third Mn(2+) in a site created by a large shift in a previously, unrecognized flap subdomain adjacent to the active site. Mutations in this, site selectively increased the Michaelis constant for Mn(2+) in the, reaction of a noncognate, small-molecule substrate, p-nitrophenyl, phosphate. The PstP/Ppp structure reveals core functional motifs that, advance the framework for understanding the mechanisms of substrate, recognition, catalysis, and regulation of PP2C phosphatases.

About this Structure

1TXO is a Single protein structure of sequence from Mycobacterium tuberculosis with MN as ligand. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.

Reference

An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase., Pullen KE, Ng HL, Sung PY, Good MC, Smith SM, Alber T, Structure. 2004 Nov;12(11):1947-54. PMID:15530359

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