Crystallization and preliminary X-ray diffraction analysis of the multidrug efflux transporter NorM from Neisseria gonorrhoeae.
The crystallization and preliminary X-ray data analysis of the NorM multidrug efflux pump produced by Neisseria gonorrhoeae are reported. NorM is a cytoplasmic membrane protein that consists of 459 amino-acid residues. It is a member of the recently classified multidrug and toxic compound extrusion (MATE) family of transporters and recognizes a number of cationic toxic compounds such as ethidium bromide, acriflavin, 2-N-methylellipticinium and ciprofloxacin. Recombinant NorM protein was expressed in Escherichia coli and purified by metal-affinity and gel-filtration chromatography. The protein was crystallized using hanging-drop vapor diffusion. X-ray diffraction data were collected from cryocooled crystals at a synchrotron light source. The best crystal diffracted anisotropically to 3.8 A and diffraction data were complete to 6.5 A resolution. The space group was determined to be C2, with unit-cell parameters a = 81.5, b = 164.4, c = 111.5 A.
Su
Chih-Chia
CC
Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
Long
Feng
F
McDermott
Gerry
G
Shafer
William M
WM
Yu
Edward W
EW
D000595:Amino Acid Sequence; D017920:Antiporters / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D009344:Neisseria gonorrhoeae / Q000737:chemistry* / Q000235:genetics
D017920:Antiporters; D001426:Bacterial Proteins; C114619:NorM protein, bacteria