view release on metacpan or  search on metacpan

t/data/good/10398587.utf8  view on Meta::CPAN

   Figure 4. Location of residues conferring resistance against triclosan.
   Stereo view of the cofactor/inhibitor binding pocket with the molecular
   surface of EnvM rendered transparent. Residues leading to triclosan
   resistance in E. coli are shown in all-bonds representation and are
   mapped in red onto the molecular surface. Phe203 forms part of the
   binding pocket near the 2-hydroxyl containing ring of triclosan, which
   can not be seen in this orientation. [125]Figure 4 has been generated
   with the program SPOCK [[126]Christopher 1998].
   [127]View Within Article
   The high-resolution structure of EnvM in complex with triclosan and
   NADH provides a framework for understanding the inhibitory mechanisms
   of triclosan in bacterial fatty acid biosynthesis. This structure
   suggests explanations for the decreased effectiveness of triclosan in
   certain E. coli strains harboring mutations in the envM gene and
   provides a model for structure based drug design of new triclosan
   derivatives lacking the toxic effects of the diazaborine inhibitors.

 §3§ Protein Data Bank accession numbers §3§

   The coordinates will be deposited in the Brookhaven Data Bank with
   accession code 1QSG, and can be requested by e-mail to:
   [128]kisker@pharm.sunysb.edu.

 §3§ Acknowledgements §3§

   This work was supported by a National Institute of Health Training
   Grant to M.J.S. and by an NIH grant to P.J.T. S.P. is a DOE/GAANN
   fellow. The NSLS in Brookhaven is supported by DOE and NIH and beamline
   X26C is supported in part by the SUNY Stony Brook Research Foundation.

 §3§ References §3§

   [129]Baldock et al 1996. C. Baldock, J.B. Rafferty, S.E. Sedelnikova,
   P.J. Baker, A.R. Stuitje, A.R. Slabas, T.R. Hawkes and D.W. Rice, A
   mechanism of drug action revealed by structural studies of enoyl
   reductase. Science 274 (1996), pp. 2107–2110. [130]Full Text via
   CrossRef | [131]View Record in Scopus | [132]Cited By in Scopus (99)

   [133]Baldock et al 1998a. C. Baldock, G.-J.D. Boer, J.B. Rafferty, A.R.
   Stuitje and D.W. Rice, Mechanism of action of diazaborines. Biochem.
   Pharm. 55 (1998), pp. 1541–1549. [134]View Record in Scopus |
   [135]Cited By in Scopus (30)

   [136]Baldock et al 1998b. C. Baldock, J.B. Rafferty, A.R. Stuitje, A.R.
   Slabas and D.W. Rice, The X-ray structure of Escherichia coli enoyl
   reductase with bound NAD^+ at 2.1 Ã… resolution. J. Mol. Biol. 284
   (1998), pp. 1529–1546. [137]Article | [138]PDF (3521 K) | [139]View
   Record in Scopus | [140]Cited By in Scopus (34)

   [141]Bhargava and Leonard 1995. H.N. Bhargava and P.A. Leonard,
   Triclosan: applications and safety. Am. J. Infect. Control 24 (1995),
   pp. 209–218.

   [142]Brunger 1992. A.T. Brünger. X-PLOR version 3.1 - A System for
   X-ray Crystallography and NMR, Yale University Press, New Haven, CT
   (1992).

   [143]Christopher 1998. J.A. Christopher. SPOCK: The Structural
   Properties Observation and Calculation Kit (Program Manual) The Center
   for Macromolecular Design, Texas A&M University, Texas, USA, College
   Station (1998).

   [144]Heath et al 1998. R.J. Heath, Y.-T. Yu, M.A. Shapiro, E. Olson and
   C.O. Rock, Broad spectrum antimicrobial biocides target the FabI
   component of fatty acid synthesis. J. Biol. Chem. 273 (1998), pp.
   30316–30320. [145]Full Text via CrossRef | [146]View Record in Scopus |
   [147]Cited By in Scopus (175)

   [148]Kraulis 1991. P.J. Kraulis, MOLSCRIPT - a program to produce both
   detailed and schematic plots of protein structures. J. Appl.
   Crystallog. 24 (1991), pp. 946–950. [149]Full Text via CrossRef

   [150]Lamzin and Wilson 1997. V.S. Lamzin and K.S. Wilson, Automated
   refinement for protein crystallography. Methods Enzymol. 277 (1997),
   pp. 269–305. [151]Abstract | [152]PDF (1777 K) | [153]View Record in
   Scopus | [154]Cited By in Scopus (244)

   [155]Laskowski et al 1993. R.A. Laskowski, M.W. McArthur, D.S. Moss and
   J.M. Thornton, PROCHECK - a program to check the stereochemical quality
   of protein structures. J. Appl. Crystallog. 26 (1993), pp. 283–291.
   [156]Full Text via CrossRef

   [157]McMurry et al 1998. L.M. McMurry, M. Oethinger and S.B. Levy,
   Triclosan targets lipid synthesis. Nature 394 (1998), pp. 531–532.
   [158]Full Text via CrossRef | [159]View Record in Scopus | [160]Cited
   By in Scopus (346)

   [161]McMurry et al 1999. L.M. McMurry, P.F. McDermott and S.B. Levy,
   Genetic evidence that InhA of Mycobacterium smegmatis is a target for
   triclosan. Antimicrob. Agents Chemother. 43 (1999), pp. 711–713.
   [162]View Record in Scopus | [163]Cited By in Scopus (114)

   [164]Merritt and Bacon 1997. E.A. Merritt and D.J. Bacon, Raster3D:
   photorealistic molecular graphics. Methods Enzymol. 277 (1997), pp.
   505–524. [165]Abstract | [166]PDF (1625 K) | [167]View Record in Scopus
   | [168]Cited By in Scopus (3507)

   [169]Murshudov et al 1997. G. Murshudov, A. Vagin and E. Dodson,
   Refinement of macromolecular structures by the maximum likelihood
   method. Acta Crystallog. sect. D 53 (1997), pp. 240–255. [170]Full Text
   via CrossRef | [171]View Record in Scopus | [172]Cited By in Scopus
   (6407)

   [173]Navaza 1994. J. Navaza, AMORE - an automated package for molecular
   replacement. Acta Crystallog. sect. A 50 (1994), pp. 157–163. [174]Full
   Text via CrossRef

   [175]Otwinowski and Minor 1997. Z. Otwinowski and W. Minor, Processing
   of X-ray diffraction data collected in oscillation mode. Methods in
   Enzymol. 276 (1997), pp. 307–326. [176]Abstract | [177]PDF (1161 K) |
   [178]View Record in Scopus | [179]Cited By in Scopus (19967)

   [180]Rozwarski et al 1998. D.A. Rozwarski, G.A. Grant, D.H.R. Barton,
   W.R.J. Jacobs and J.C. Sacchettini, Modification of the NADH of the
   isoniazid target (InhA) from Mycobacterium tuberculosis. Science 279
   (1998), pp. 98–102. [181]Full Text via CrossRef | [182]View Record in
   Scopus | [183]Cited By in Scopus (291)

   [184]Saito et al 1981. K. Saito, A. Kawaguchi, Y. Seyama, T. Yamakawa
   and S. Okuda, Steric course of reaction catalyzed by the enoyl