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@ARTICLE{Priya:142572,
      author       = {Priya, R. and Biukovic, G. and Manimekalai, M. and Lim, J.
                      and Rao, S. S. and Grueber, G. and DESY},
      title        = {{S}olution structure of subunit ($\gamma$ ($\gamma$1-204))
                      of the {M}ycobacterium tuberculosis {F}-{ATP} synthase and
                      the unique loop of ($\gamma$165-178), representing a novel
                      {TB} drug target},
      journal      = {Journal of bioenergetics and biomembranes},
      volume       = {45},
      issn         = {0145-479X},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {PHPPUBDB-25512},
      pages        = {1-9},
      year         = {2013},
      note         = {© Springer Science+Business Media New York; Post referee
                      fulltext in progress; Embargo 12 months from publication},
      abstract     = {Tuberculosis, caused by the strain Mycobacterium
                      tuberculosis, is in focus of interest due to the emergence
                      of multi- and extensive drug-resistant TB strains. The
                      F(1)F(O) ATP synthase is one of the essential enzymes in
                      energy requirement of both proliferating aerobic and hypoxic
                      dormant stage of mycobacterium life cycle, and therefore a
                      potential TB drug target. Subunit γ of F-ATP synthases
                      plays an important role in coupling and catalysis via
                      conformational transitions of its N- and C-termini as well
                      as the bottom segment of the globular domain of γ, which is
                      in close proximity to the rotating and ion-pumping c-ring.
                      Here we describe the first production, purification and low
                      resolution solution structure of subunit γ (γ(1-204),
                      Mtγ(1-204)) of the M. tuberculosis F-ATP synthase.
                      Mtγ(1-204) is a pear-like shaped protein with a molecular
                      weight of 23 ± 2 kDa. Protein sequence analysis of Mtγ
                      revealed differences in the amino acid composition to γ
                      subunits from other sources, in particular the presence of a
                      unique stretch of 13 amino acid residues (Mtγ(165-178)).
                      NMR studies showed that Mtγ(165-178) forms a loop of polar
                      residues. Mtγ(165-178) has been aligned at the bottom of
                      the globular domain of the Escherichia coli subunit γ,
                      being in close vicinity to the polar residues R41, Q42, E44
                      and Q46 (M. tuberculosis nomenclature) of the c-ring. The
                      putative role(s) of Mtγ(165-178) in coupling and as a
                      potential drug target are discussed.},
      keywords     = {Antitubercular Agents: chemistry / Antitubercular Agents:
                      therapeutic use / Bacterial Proteins: antagonists $\&$
                      inhibitors / Bacterial Proteins: chemistry / Bacterial
                      Proteins: genetics / Bacterial Proteins: metabolism /
                      Catalysis / Drug Delivery Systems / Enzyme Inhibitors:
                      chemistry / Enzyme Inhibitors: therapeutic use /
                      Mycobacterium tuberculosis: enzymology / Mycobacterium
                      tuberculosis: genetics / Nuclear Magnetic Resonance,
                      Biomolecular / Protein Structure, Secondary / Protein
                      Subunits: antagonists $\&$ inhibitors / Protein Subunits:
                      chemistry / Protein Subunits: diagnostic use / Protein
                      Subunits: metabolism / Proton-Translocating ATPases:
                      antagonists $\&$ inhibitors / Proton-Translocating ATPases:
                      chemistry / Proton-Translocating ATPases: genetics /
                      Proton-Translocating ATPases: metabolism / Recombinant
                      Proteins: antagonists $\&$ inhibitors / Recombinant
                      Proteins: chemistry / Recombinant Proteins: genetics /
                      Recombinant Proteins: metabolism / Tuberculosis: drug
                      therapy / Tuberculosis: enzymology / Antitubercular Agents
                      (NLM Chemicals) / Bacterial Proteins (NLM Chemicals) /
                      Enzyme Inhibitors (NLM Chemicals) / Protein Subunits (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) /
                      Proton-Translocating ATPases (NLM Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23104121},
      UT           = {WOS:000314899500011},
      doi          = {10.1007/s10863-012-9486-4},
      url          = {https://bib-pubdb1.desy.de/record/142572},
}