Journal Article

PHPPUBDB-25737

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural characterization of the multidomain regulatory protein Rv1364c from mycobacterium tuberculosis

King-scott, J. ; Konarev, P. V. ; Panjikar, S. ; Jordanova, R. ; Svergun, D. I. ; Tucker, P. A. ; DESY

2011
Elsevier Science London [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.str.2010.11.010

Abstract: The open reading frame rv1364c of Mycobacterium tuberculosis, which regulates the stress-dependent σ factor, σ(F), has been analyzed structurally and functionally. Rv1364c contains domains with sequence similarity to the RsbP/RsbW/RsbV regulatory system of the stress-response σ factor of Bacillus subtilis. Rv1364c contains, sequentially, a PAS domain (which shows sequence similarity to the PAS domain of the B. subtilis RsbP protein), an active phosphatase domain, a kinase (anti-σ(F) like) domain and a C-terminal anti-σ(F) antagonist like domain. The crystal structures of two PAS domain constructs (at 2.3 and 1.6 Å) and a phosphatase/kinase dual domain construct (at 2.6 Å) are described. The PAS domain is shown to bind palmitic acid but to have 100 times greater affinity for palmitoleic acid. The full-length protein can exist in solution as both monomer and dimer. We speculate that a switch between monomer and dimer, possibly resulting from fatty acid binding, affects the accessibility of the serine of the C-terminal, anti-σ(F) antagonist domain for dephosphorylation by the phosphatase domain thus indirectly altering the availability of σ(F).

Keyword(s): Bacterial Proteins: chemistry (MeSH) ; Binding Sites (MeSH) ; Catalytic Domain (MeSH) ; Crystallography, X-Ray (MeSH) ; Enzyme Assays (MeSH) ; Fatty Acids: metabolism (MeSH) ; Humans (MeSH) ; Kinetics (MeSH) ; Mycobacterium tuberculosis: enzymology (MeSH) ; Phosphotransferases: chemistry (MeSH) ; Protein Binding (MeSH) ; Protein Multimerization (MeSH) ; Protein Structure, Tertiary (MeSH) ; Protein-Serine-Threonine Kinases: chemistry (MeSH) ; Scattering, Small Angle (MeSH) ; Structural Homology, Protein (MeSH) ; X-Ray Diffraction (MeSH) ; Bacterial Proteins ; Fatty Acids ; Phosphotransferases ; PAS domain kinases ; Protein-Serine-Threonine Kinases

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Contributing Institute(s):

1. European Molecular Biology Laboratory (EMBL)

Research Program(s):

1. DORIS Beamline K1.2 (POF2-54G13) (POF2-54G13)
2. DORIS Beamline BW7 (POF2-54G13) (POF2-54G13)
3. DORIS Beamline K1.1 (POF2-54G13) (POF2-54G13)

Experiment(s):

1. DORIS Beamline K1.1 (DORIS III)
2. DORIS Beamline BW7 (DORIS III)
3. DORIS Beamline K1.2 (DORIS III)

Appears in the scientific report 2011
Notes: (c) Elsevier Ltd. Post referee fulltext in progress.

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Database coverage:
; No Author Disambiguation

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