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@ARTICLE{Mokranjac:81236,
      author       = {Mokranjac, Dejana and Bourenkov, Gleb and Hell, Kai and
                      Neupert, Walter and Groll, Michael},
      title        = {{S}tructure and function of {T}im14 and {T}im16, the {J}
                      and {J}-like components of the mitochondrial protein import
                      motor},
      journal      = {The EMBO journal},
      volume       = {25},
      number       = {19},
      issn         = {0261-4189},
      address      = {Hoboken, NJ [u.a.]},
      publisher    = {Wiley},
      reportid     = {PHPPUBDB-3315},
      pages        = {4675-4685},
      year         = {2006},
      abstract     = {The import motor of the mitochondrial translocase of the
                      inner membrane (TIM23) mediates the ATP-dependent
                      translocation of preproteins into the mitochondrial matrix
                      by cycles of binding to and release from mtHsp70. An
                      essential step of this process is the stimulation of the
                      ATPase activity of mtHsp70 performed by the J cochaperone
                      Tim14. Tim14 forms a complex with the J-like protein Tim16.
                      The crystal structure of this complex shows that the
                      conserved domains of the two proteins have virtually
                      identical folds but completely different surfaces enabling
                      them to perform different functions. The Tim14-Tim16 dimer
                      reveals a previously undescribed arrangement of J and J-like
                      domains. Mutations that destroy the complex between Tim14
                      and Tim16 are lethal demonstrating that complex formation is
                      an essential requirement for the viability of cells. We
                      further demonstrate tight regulation of the cochaperone
                      activity of Tim14 by Tim16. The first crystal structure of a
                      J domain in complex with a regulatory protein provides new
                      insights into the function of the mitochondrial TIM23
                      translocase and the Hsp70 chaperone system in general.},
      keywords     = {Amino Acid Sequence / Crystallography, X-Ray / Dimerization
                      / Evolution, Molecular / Membrane Transport Proteins:
                      chemistry / Membrane Transport Proteins: metabolism /
                      Mitochondrial Membrane Transport Proteins / Mitochondrial
                      Proteins: chemistry / Mitochondrial Proteins: metabolism /
                      Models, Molecular / Molecular Motor Proteins: chemistry /
                      Molecular Motor Proteins: metabolism / Molecular Sequence
                      Data / Protein Structure, Secondary / Protein Structure,
                      Tertiary / Protein Subunits: chemistry / Protein Subunits:
                      metabolism / Protein Transport / Saccharomyces cerevisiae:
                      chemistry / Saccharomyces cerevisiae: metabolism /
                      Saccharomyces cerevisiae Proteins: chemistry / Saccharomyces
                      cerevisiae Proteins: metabolism / Sequence Alignment /
                      Structure-Activity Relationship / Membrane Transport
                      Proteins (NLM Chemicals) / Mitochondrial Membrane Transport
                      Proteins (NLM Chemicals) / Mitochondrial Proteins (NLM
                      Chemicals) / Molecular Motor Proteins (NLM Chemicals) /
                      Pam16 protein, S cerevisiae (NLM Chemicals) / Protein
                      Subunits (NLM Chemicals) / Saccharomyces cerevisiae Proteins
                      (NLM Chemicals) / Tim14 protein, S cerevisiae (NLM
                      Chemicals)},
      cin          = {MPG(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)MPG_-2012_-20120307$},
      pnm          = {DORIS Beamline BW6 (POF1-550)},
      pid          = {G:(DE-H253)POF1-BW6-20130405},
      experiment   = {EXP:(DE-H253)D-BW6-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16977310},
      pmc          = {pmc:PMC1590002},
      UT           = {WOS:000241078000025},
      doi          = {10.1038/sj.emboj.7601334},
      url          = {https://bib-pubdb1.desy.de/record/81236},
}