Crystallization and preliminary crystallographic analysis of decameric and monomeric forms of C49S mutant thioredoxin-dependent AhpC from Helicobacter pylori.
Cys49Ser mutant Helicobacter pylori alkyl hydroperoxide reductase (C49S HpAhpC) was purified under reducing conditions in monomeric and decameric forms. The monomeric form was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.25 A resolution and belonged to space group C2, with unit-cell parameters a = 245.8, b = 140.7, c = 189.5 A, beta = 127 degrees , and contained 20 molecules in the asymmetric unit. A crystal of the decameric form was obtained by the microbatch crystallization method and diffracted to 2.8 A resolution. It belonged to space group C222, with unit-cell parameters a = 257.5, b = 417.5, c = 95.6 A. The structure of the monomeric form of C49S HpAhpC has been solved by the molecular-replacement method.
Division of Applied Life Science (BK21 Program), Gyeongsang National University, Jinju 660-701, Republic of Korea.
Seo
Kyung Hye
KH
Furqoni
Ahmad
A
Kwon
Young Chul
YC
Cho
Myung Je
MJ
Rhee
Kwang Ho
KH
Lee
Sang Yeol
SY
Lee
Kon Ho
KH
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017354:Point Mutation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D010544:Peroxidases; C508531:ahpC protein, Helicobacter pylori