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Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSerine/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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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