Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2004 Nov;12(11):1947-54.
doi: 10.1016/j.str.2004.09.008.

An Alternate Conformation and a Third Metal in PstP/Ppp, the M. Tuberculosis PP2C-Family Ser/Thr Protein Phosphatase

Affiliations
Free article

An Alternate Conformation and a Third Metal in PstP/Ppp, the M. Tuberculosis PP2C-Family Ser/Thr Protein Phosphatase

Kristi E Pullen et al. Structure. .
Free article

Abstract

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.

Comment in

Similar articles

See all similar articles

Cited by 43 articles

See all "Cited by" articles

Publication types

MeSH terms

Substances

Associated data

LinkOut - more resources

Feedback