TY - JOUR
AU - King-scott, J.
AU - Konarev, P. V.
AU - Panjikar, S.
AU - Jordanova, R.
AU - Svergun, D. I.
AU - Tucker, P. A.
AU - DESY
TI - Structural characterization of the multidomain regulatory protein Rv1364c from mycobacterium tuberculosis
JO - Structure
VL - 19
SN - 0969-2126
CY - London [u.a.]
PB - Elsevier Science
M1 - PHPPUBDB-25737
SP - 56
PY - 2011
AB - 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).
KW - Bacterial Proteins: chemistry
KW - Binding Sites
KW - Catalytic Domain
KW - Crystallography, X-Ray
KW - Enzyme Assays
KW - Fatty Acids: metabolism
KW - Humans
KW - Kinetics
KW - Mycobacterium tuberculosis: enzymology
KW - Phosphotransferases: chemistry
KW - Protein Binding
KW - Protein Multimerization
KW - Protein Structure, Tertiary
KW - Protein-Serine-Threonine Kinases: chemistry
KW - Scattering, Small Angle
KW - Structural Homology, Protein
KW - X-Ray Diffraction
KW - Bacterial Proteins (NLM Chemicals)
KW - Fatty Acids (NLM Chemicals)
KW - Phosphotransferases (NLM Chemicals)
KW - PAS domain kinases (NLM Chemicals)
KW - Protein-Serine-Threonine Kinases (NLM Chemicals)
LB - PUB:(DE-HGF)16
C6 - pmid:21220116
UR - <Go to ISI:>//WOS:000286348000009
DO - DOI:10.1016/j.str.2010.11.010
UR - https://bib-pubdb1.desy.de/record/144029
ER -