1TXO

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

Summary for 1TXO

• Entry DOI: 10.2210/pdb1txo/pdb
• Descriptor: Putative Bacterial Enzyme, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: putative bacterial enzyme, serine/threonine protein phosphatases, pstp/ppp, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, hydrolase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 51296.93

Authors

Pullen, K.E.,Ng, H.L.,Sung, P.Y.,Good, M.C.,Smith, S.M.,Alber, T.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2004-07-05, release date: 2004-11-23, Last modification date: 2024-10-30)

Primary citation

Pullen, K.E.,Ng, H.L.,Sung, P.Y.,Good, M.C.,Smith, S.M.,Alber, T.
An Alternate Conformation and a Third Metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr Protein Phosphatase.
Structure, 12:1947-1954, 2004

PubMed 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.

PubMed: 15530359
DOI: 10.1016/j.str.2004.09.008

Experimental method

X-RAY DIFFRACTION (1.95 Å)