An Alternate Conformation and a Third Metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr Protein Phosphatase-Reference-Cited by-同舟云学术

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

Published:2004-11 Issue:11 Volume:12 Page:1947-1954
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Pullen Kristi E.,Ng Ho-Leung,Sung Pei-Yi,Good Matthew C.,Smith Stephen M.,Alber Tom

Funder

University of California

National Science Foundation

National Institutes of Health

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference34 articles.

1. The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis;Av-Gay;Trends Microbiol,2000

2. Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB;Av-Gay;Infect. Immun,1999

3. The structure and mechanism of protein phosphatases;Barford;Annu. Rev. Biophys. Biomol. Struct,1998

4. Susceptibility to mycobacterial infections;Bellamy;Genes Immun,2003

5. PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis;Boitel;Mol. Microbiol,2003

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1. Docking interactions determine substrate specificity of members of a widespread family of protein phosphatases;Journal of Biological Chemistry;2024-09

2. Crystal structure and mechanistic studies of the PPM1D serine/threonine phosphatase catalytic domain;Journal of Biological Chemistry;2024-08

3. Docking interactions determine substrate specificity of members of a widespread family of protein phosphatases;2024-05-05

4. Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state;Nature Communications;2022-06-30

5. Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism;Molecular Microbiology;2022-06-20

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