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@ARTICLE{Kingscott:144029,
      author       = {King-scott, J. and Konarev, P. V. and Panjikar, S. and
                      Jordanova, R. and Svergun, D. I. and Tucker, P. A. and DESY},
      title        = {{S}tructural characterization of the multidomain regulatory
                      protein {R}v1364c from mycobacterium tuberculosis},
      journal      = {Structure},
      volume       = {19},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PHPPUBDB-25737},
      pages        = {56},
      year         = {2011},
      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).},
      keywords     = {Bacterial Proteins: chemistry / Binding Sites / Catalytic
                      Domain / Crystallography, X-Ray / Enzyme Assays / Fatty
                      Acids: metabolism / Humans / Kinetics / Mycobacterium
                      tuberculosis: enzymology / Phosphotransferases: chemistry /
                      Protein Binding / Protein Multimerization / Protein
                      Structure, Tertiary / Protein-Serine-Threonine Kinases:
                      chemistry / Scattering, Small Angle / Structural Homology,
                      Protein / X-Ray Diffraction / Bacterial Proteins (NLM
                      Chemicals) / Fatty Acids (NLM Chemicals) /
                      Phosphotransferases (NLM Chemicals) / PAS domain kinases
                      (NLM Chemicals) / Protein-Serine-Threonine Kinases (NLM
                      Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline K1.2 (POF2-54G13) / DORIS Beamline BW7
                      (POF2-54G13) / DORIS Beamline K1.1 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.2-20130405 /
                      G:(DE-H253)POF2-BW7-20130405 /
                      G:(DE-H253)POF2-K1.1-20130405},
      experiment   = {EXP:(DE-H253)D-K1.1-20150101 / EXP:(DE-H253)D-BW7-20150101
                      / EXP:(DE-H253)D-K1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21220116},
      UT           = {WOS:000286348000009},
      doi          = {10.1016/j.str.2010.11.010},
      url          = {https://bib-pubdb1.desy.de/record/144029},
}