%0 Journal Article
%A King-scott, J.
%A Konarev, P. V.
%A Panjikar, S.
%A Jordanova, R.
%A Svergun, D. I.
%A Tucker, P. A.
%A DESY
%T Structural characterization of the multidomain regulatory protein Rv1364c from mycobacterium tuberculosis
%J Structure
%V 19
%@ 0969-2126
%C London [u.a.]
%I Elsevier Science
%M PHPPUBDB-25737
%P 56
%D 2011
%X 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).
%K Bacterial Proteins: chemistry
%K Binding Sites
%K Catalytic Domain
%K Crystallography, X-Ray
%K Enzyme Assays
%K Fatty Acids: metabolism
%K Humans
%K Kinetics
%K Mycobacterium tuberculosis: enzymology
%K Phosphotransferases: chemistry
%K Protein Binding
%K Protein Multimerization
%K Protein Structure, Tertiary
%K Protein-Serine-Threonine Kinases: chemistry
%K Scattering, Small Angle
%K Structural Homology, Protein
%K X-Ray Diffraction
%K Bacterial Proteins (NLM Chemicals)
%K Fatty Acids (NLM Chemicals)
%K Phosphotransferases (NLM Chemicals)
%K PAS domain kinases (NLM Chemicals)
%K Protein-Serine-Threonine Kinases (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:21220116
%U <Go to ISI:>//WOS:000286348000009
%R 10.1016/j.str.2010.11.010
%U https://bib-pubdb1.desy.de/record/144029