title: Crystallization and preliminary X-ray crystallographic analysis of the tetracycline-degrading monooxygenase TetX2 from Bacteroides thetaiotaomicron.
abstract: The flavin-dependent monooxygenase TetX2 from Bacteroides thetaiotaomicron confers resistance against tetracyclines in aerobically grown Escherichia coli. TetX2 modifies several tetracycline antibiotics by regioselective hydroxylation of the substrates to 11a-hydroxy-tetracyclines. X-ray diffraction data were collected from a native TetX2 crystal and a TetX2 crystal with incorporated selenomethionine to resolutions of 2.5 and 3.0 A, respectively. The native crystal belonged to the triclinic space group P1, with unit-cell parameters a = 68.55, b = 80.88, c = 87.53 A, alpha = 111.09, beta = 98.98, gamma = 93.38 degrees , whereas the selenomethionine-labelled TetX2 crystal belonged to the monoclinic space group P2(1), with unit-cell parameters a = 87.34, b = 68.66, c = 152.48 A, beta = 101.08 degrees .
authors.affiliation: Institut für Biochemie, Universität Greifswald, Felix-Hausdorff-Strasse 4, D-17489 Greifswald, Germany. gesa.volkers@uni-greifswald.de
authors.forename: Gesa
authors.initials: G
authors.lastname: Volkers
authors.forename: Linda
authors.initials: L
authors.lastname: Schuldt
authors.forename: Gottfried J
authors.initials: GJ
authors.lastname: Palm
authors.forename: Gerard D
authors.initials: GD
authors.lastname: Wright
authors.forename: Winfried
authors.initials: W
authors.lastname: Hinrichs
mesh_terms: D001439:Bacteroides / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism; D013752:Tetracycline / Q000378:metabolism
chemical_list: D006899:Mixed Function Oxygenases; D013752:Tetracycline
references.citation: J Biol Chem. 2004 Dec 10;279(50):52346-52
references.pmid: 15452119
references.citation: Anal Biochem. 1996 May 1;236(2):302-8
references.pmid: 8660509
references.citation: Biochemistry. 2005 Sep 6;44(35):11829-35
references.pmid: 16128584
references.citation: Ann N Y Acad Sci. 1948 Nov 30;51(Art. 2):177-81
references.pmid: 18112227
references.citation: Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):2023-30
references.pmid: 14573958
references.citation: Methods Enzymol. 1997;276:307-26
references.pmid: 27754618
references.citation: Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):965-72
references.pmid: 10944333
references.citation: J Synchrotron Radiat. 2004 Jan 1;11(Pt 1):56-9
references.pmid: 14646134
references.citation: Acta Crystallogr D Biol Crystallogr. 1999 Oct;55(Pt 10):1718-25
references.pmid: 10531521
references.citation: Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
references.pmid: 15572765
references.citation: Science. 1991 Oct 4;254(5028):51-8
references.pmid: 1925561
references.citation: J Mol Biol. 1968 Apr 28;33(2):491-7
references.pmid: 5700707
references.citation: Acta Crystallogr A. 2008 Jan;64(Pt 1):112-22
references.pmid: 18156677
references.citation: EMBO J. 2001 Apr 17;20(8):1829-39
references.pmid: 11296217
references.citation: Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):449-57
references.pmid: 15805600
references.citation: Cell Mol Life Sci. 2010 Feb;67(3):419-31
references.pmid: 19862477
references.citation: J Bacteriol. 1988 Apr;170(4):1423-9
references.pmid: 2832361
references.citation: J Appl Microbiol. 2009 Apr;106(4):1336-42
references.pmid: 19187139