Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Haloferax mediterranei

被引:9
作者
Ferrer, J
Fisher, M
Burke, J
Sedelnikova, SE
Baker, PJ
Gilmour, DJ
Bonete, MJ
Pire, C
Esclapez, J
Rice, DW [1 ]
机构
[1] Univ Sheffield, Krebs Inst Biomolec Res, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England
[2] Univ Alicante, Fac Ciencias, Dept Agroquim & Bioquim, E-03080 Alicante, Spain
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2001年 / 57卷
关键词
D O I
10.1107/S0907444901015189
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Glucose dehydrogenase (E.C 1.1.1.47; GlcDH) from Haloferax mediterranei has been overexpressed in Escherichia coli, solubilized by the addition of 8 M urea and refolded by rapid dilution. The protein has been purified by conventional techniques and crystallized by the hanging-drop vapour-diffusion method using sodium citrate as the precipitant. Two crystal forms representing the free enzyme and the binary complex with NADP(+) grow under these conditions. Crystals of form I diffract to beyond 3.5 Angstrom resolution and belong to the hexagonal space group P622, with unit-cell parameters a=b=89.1, c=214.6 Angstrom, alpha=beta =90, gamma =120 degrees. Crystals of form II diffract to greater than 2.0 Angstrom and belong to the orthorhombic space group I222 or I2(1)2(1)2(1), with unit-cell parameters a=61.8, b=110.9, c=151.7 Angstrom, alpha=beta=gamma =90 degrees. Calculated values for V-M and consideration of the packing for both crystal forms suggests that the asymmetric units in both crystal forms contain a monomer.
引用
收藏
页码:1887 / 1889
页数:3
相关论文
共 14 条
[1]  
[Anonymous], PROTEINS
[2]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[3]   Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterisation and N-terminal sequence [J].
Bonete, MJ ;
Pire, C ;
LLorca, FI ;
Camacho, ML .
FEBS LETTERS, 1996, 383 (03) :227-229
[4]   Insights into the molecular basis of salt tolerance from the study of glutamate dehydrogenase from Halobacterium salinarum [J].
Britton, KL ;
Stillman, TJ ;
Yip, KSP ;
Forterre, P ;
Engel, PC ;
Rice, DW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (15) :9023-9030
[5]   CENTRAL METABOLISM OF THE ARCHAEBACTERIA - AN OVERVIEW [J].
DANSON, MJ .
CANADIAN JOURNAL OF MICROBIOLOGY, 1989, 35 (01) :58-64
[6]   STRUCTURAL FEATURES THAT STABILIZE HALOPHILIC MALATE-DEHYDROGENASE FROM AN ARCHAEBACTERIUM [J].
DYM, O ;
MEVARECH, M ;
SUSSMAN, JL .
SCIENCE, 1995, 267 (5202) :1344-1346
[7]   Structural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases [J].
Edwards, KJ ;
Barton, JD ;
Rossjohn, J ;
Thorn, JM ;
Taylor, GL ;
Ollis, DL .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1996, 328 (01) :173-183
[8]   BIOCHEMICAL, STRUCTURAL, AND MOLECULAR-GENETIC ASPECTS OF HALOPHILISM [J].
EISENBERG, H ;
MEVARECH, M ;
ZACCAI, G .
ADVANCES IN PROTEIN CHEMISTRY, 1992, 43 :1-62
[9]   MICROBIAL BEHAVIOR IN SALT-STRESSED ECOSYSTEMS [J].
GALINSKI, EA ;
TRUPER, HG .
FEMS MICROBIOLOGY REVIEWS, 1994, 15 (2-3) :95-108
[10]   THE CRYSTAL-STRUCTURE OF GLUCOSE-DEHYDROGENASE FROM THERMOPLASMA-ACIDOPHILUM [J].
JOHN, J ;
CRENNELL, SJ ;
HOUGH, DW ;
DANSON, MJ ;
TAYLOR, GL .
STRUCTURE, 1994, 2 (05) :385-393