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@ARTICLE{Bokhove:95792,
      author       = {Bokhove, M. and Yoshida, H. and Hensgens, C. M. H. and van
                      der Laan, J. M. and Sutherland, J. D. and Dijkstra, B. W.
                      and DESY},
      title        = {{S}tructures of an isopenicillin {N} converting
                      {N}tn-hydrolase reveal different catalytic roles for the
                      active site residues of precursor and mature enzyme.},
      journal      = {Structure},
      volume       = {18},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PHPPUBDB-19255},
      pages        = {301-308},
      year         = {2010},
      abstract     = {Penicillium chrysogenum Acyl coenzyme A:isopenicillin N
                      acyltransferase (AT) performs the last step in the
                      biosynthesis of hydrophobic penicillins, exchanging the
                      hydrophilic side chain of a precursor for various
                      hydrophobic side chains. Like other N-terminal nucleophile
                      hydrolases AT is produced as an inactive precursor that
                      matures upon posttranslational cleavage. The structure of a
                      Cys103Ala precursor mutant shows that maturation is
                      autoproteolytic, initiated by Cys103 cleaving its preceding
                      peptide bond. The crystal structure of the mature enzyme
                      shows that after autoproteolysis residues 92-102 fold
                      outwards, exposing a buried pocket. This pocket is
                      structurally and chemically flexible and can accommodate
                      substrates of different size and polarity. Modeling of a
                      substrate-bound state indicates the residues important for
                      catalysis. Comparison of the proposed autoproteolytic and
                      substrate hydrolysis mechanisms shows that in both events
                      the same catalytic residues are used, but that they perform
                      different roles in catalysis.},
      keywords     = {Acyltransferases: chemistry / Acyltransferases: metabolism
                      / Amidohydrolases: chemistry / Amidohydrolases: metabolism /
                      Catalysis / Catalytic Domain / Crystallography, X-Ray /
                      Cysteine: chemistry / Cysteine: metabolism / Hydrolysis /
                      Models, Molecular / Penicillin-Binding Proteins: chemistry /
                      Penicillin-Binding Proteins: metabolism / Penicillins:
                      chemistry / Penicillins: metabolism / Protein Conformation /
                      Penicillin-Binding Proteins (NLM Chemicals) / Penicillins
                      (NLM Chemicals) / Cysteine (NLM Chemicals) /
                      Acyltransferases (NLM Chemicals) /
                      acyl-CoA-6-aminopenicillanic acid acyltransferase (NLM
                      Chemicals) / Amidohydrolases (NLM Chemicals) / N-terminal
                      nucleophile hydrolase (NLM Chemicals) / penicillin N (NLM
                      Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline BW7 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW7-20130405},
      experiment   = {EXP:(DE-H253)D-BW7-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20223213},
      UT           = {WOS:000275492000007},
      doi          = {10.1016/j.str.2010.01.005},
      url          = {https://bib-pubdb1.desy.de/record/95792},
}