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@ARTICLE{Syson:207454,
      author       = {Syson, Karl and Stevenson, Clare E. M. and Rashid, Abdul M.
                      and Saalbach, Gerhard and Tang, Minhong and Tuukkanen, Anne
                      and Svergun, Dmitri and Withers, Stephen G. and Lawson,
                      David M. and Bornemann, Stephen},
      title        = {{S}tructural {I}nsight into {H}ow {S}treptomyces coelicolor
                      {M}altosyl {T}ransferase {G}lg{E} {B}inds $\alpha$-{M}altose
                      1-{P}hosphate and {F}orms a {M}altosyl-{E}nzyme
                      {I}ntermediate},
      journal      = {Biochemistry},
      volume       = {53},
      number       = {15},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PUBDB-2015-01352},
      pages        = {2494 - 2504},
      year         = {2014},
      abstract     = {GlgE (EC 2.4.99.16) is an α-maltose
                      1-phosphate:(1→4)-α- D -glucan 4-α- D
                      -maltosyltransferase of theCAZy glycoside hydrolase $13_3$
                      family. It is the definingenzyme of a bacterial α-glucan
                      biosynthetic pathway and is agenetically validated
                      anti-tuberculosis target. It catalyzes the α-retaining
                      transfer of maltosyl units from α-maltose 1-phosphate to
                      maltooligosaccharides and is predicted to use
                      adouble-displacement mechanism. Evidence of this
                      mechanismwas obtained using a combination of site-directed
                      mutagenesis of Streptomyces coelicolor GlgE isoform I,
                      substrate analogues,protein crystallography, and mass
                      spectrometry. The X-ray structures of α-maltose 1-phosphate
                      bound to a D394A mutein and
                      aβ-2-deoxy-2-fluoromaltosyl-enzyme intermediate with a
                      E423A mutein were determined. There are few examples of
                      CAZyglycoside hydrolase family 13 members that have had
                      their glycosyl-enzyme intermediate structures determined,
                      and none beforenow have been obtained with a
                      2-deoxy-2-fluoro substrate analogue. The covalent
                      modification of Asp394 was confirmed usingmass spectrometry.
                      A similar modification of wild-type GlgE proteins from S.
                      coelicolor and Mycobacterium tuberculosis was alsoobserved.
                      Small-angle X-ray scattering of the M. tuberculosis enzyme
                      revealed a homodimeric assembly similar to that of the
                      S.coelicolor enzyme but with slightly differently oriented
                      monomers. The deeper understanding of the
                      structure−functionrelationships of S. coelicolor GlgE will
                      aid the development of inhibitors of the M. tuberculosis
                      enzyme.},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13) / ELISA - European Light
                      Sources Activities - Synchrotrons and Free Electron Lasers
                      (226716)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405 / G:(EU-Grant)226716},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000334991100008},
      pubmed       = {pmid:24689960},
      doi          = {10.1021/bi500183c},
      url          = {https://bib-pubdb1.desy.de/record/207454},
}