% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Shi:823944,
      author       = {Shi, Jie and Cao, Xinyun and Chen, Yaozong and Cronan, John
                      E. and Guo, Zhihong},
      title        = {{A}n {A}typical α/β-{H}ydrolase {F}old {R}evealed in the
                      {C}rystal {S}tructure of {P}imeloyl-{A}cyl {C}arrier
                      {P}rotein {M}ethyl {E}sterase {B}io{G} from {H}aemophilus
                      influenzae},
      journal      = {Biochemistry},
      volume       = {55},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2016-06572},
      pages        = {6705-6717},
      year         = {2016},
      abstract     = {Pimeloyl-acyl carrier protein (ACP) methyl esterase is an
                      α/β-hydrolase that catalyzes the last biosynthetic step of
                      pimeloyl-ACP, a key intermediate in biotin biosynthesis.
                      Intriguingly, multiple nonhomologous isofunctional forms of
                      this enzyme that lack significant sequence identity are
                      present in diverse bacteria. One such esterase, Escherichia
                      coli BioH, has been shown to be a typical α/β-hydrolase
                      fold enzyme. To gain further insights into the role of this
                      step in biotin biosynthesis, we have determined the crystal
                      structure of another widely distributed pimeloyl-ACP methyl
                      esterase, Haemophilus inf luenzae BioG, at 1.26 Å. The BioG
                      structure is similar to the BioH structure and is composed
                      of an α-helical lid domain and a core domain that contains
                      a central sevenstranded β-pleated sheet. However, four of
                      the six α-helices that flank both sides of the BioH core
                      β-sheet are replaced with long loops in BioG, thus forming
                      an unusual α/β-hydrolase fold. This structural variation
                      results in a significantly decreased thermal stability of
                      the enzyme. Nevertheless, the lid domain and the residues at
                      the lid−core interface are well conserved between BioH and
                      BioG, in which an analogous hydrophobic pocket for pimelate
                      binding as well as similar ionic interactions with the ACP
                      moiety are retained. Biochemical characterization of
                      sitedirected mutants of the residues hypothesized to
                      interact with the ACP moiety supports a similar substrate
                      interaction mode for the two enzymes. Consequently, these
                      enzymes package the identical catalytic function under a
                      considerably different protein surface.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000389557300012},
      doi          = {10.1021/acs.biochem.6b00818},
      url          = {https://juser.fz-juelich.de/record/823944},
}