CRYSTAL-STRUCTURE OF ESCHERICHIA-COLI QOR QUINONE OXIDOREDUCTASE COMPLEXED WITH NADPH

被引:98
作者
THORN, JM [1 ]
BARTON, JD [1 ]
DIXON, NE [1 ]
OLLIS, DL [1 ]
EDWARDS, KJ [1 ]
机构
[1] AUSTRALIAN NATL UNIV,RES SCH CHEM,CTR MOLEC STRUCT & FUNCT,CANBERRA,ACT 0200,AUSTRALIA
关键词
QUINONE OXIDOREDUCTASE; ALCOHOL DEHYDROGENASE; ZETA-CRYSTALLIN; CRYSTAL STRUCTURE; NADPH;
D O I
10.1006/jmbi.1995.0337
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of the homodimer of quinone oxidoreductase from Escherichia coli has been determined using the multiple isomorphous replacement method at 2.2 Angstrom resolution and refined to an R-factor of 14.1% The crystallographic asymmetric unit contains one functional dimer with the two subunits being related by a non-crystallographic 2-fold symmetry axis. The model consists of two polypeptide chains (residues 2 through 327), one NADPH molecule and one sulphate anion per subunit, and 432 water molecules. Each subunit consists of two domains: a catalytic domain and a nucleotide-binding domain with the NADPH co-factor bound in the cleft between domains. Quinone oxidoreductase has an unusual nucleotide-binding fingerprint motif consisting of the sequence AXXGXXG. The overall structure of quinone oxidoreductase shows strong structural homology to that of horse liver alcohol dehydrogenase.
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页码:785 / 799
页数:15
相关论文
共 33 条
  • [1] BELLOMO G, 1987, CHEM SCRIPTA, V27A, P117
  • [2] PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES
    BERNSTEIN, FC
    KOETZLE, TF
    WILLIAMS, GJB
    MEYER, EF
    BRICE, MD
    RODGERS, JR
    KENNARD, O
    SHIMANOUCHI, T
    TASUMI, M
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1977, 112 (03) : 535 - 542
  • [3] EYE LENS ZETA-CRYSTALLIN RELATIONSHIPS TO THE FAMILY OF LONG-CHAIN ALCOHOL POLYOL DEHYDROGENASES - PROTEIN TRIMMING AND CONSERVATION OF STABLE PARTS
    BORRAS, T
    PERSSON, B
    JORNVALL, H
    [J]. BIOCHEMISTRY, 1989, 28 (15) : 6133 - 6139
  • [4] BRUNGER AT, 1992, X PLOR V3 1 MANUAL S
  • [5] CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES ON A SOLUBLE ESCHERICHIA-COLI QUINONE OXIDOREDUCTASE
    EDWARDS, KJ
    THORN, JM
    DANIHER, JA
    DIXON, NE
    OLLIS, DL
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1994, 240 (05) : 501 - 503
  • [6] MOLECULAR ASPECTS OF FUNCTIONAL DIFFERENCES BETWEEN ALCOHOL AND SORBITOL DEHYDROGENASES
    EKLUND, H
    HORJALES, E
    JORNVALL, H
    BRANDEN, CI
    JEFFERY, J
    [J]. BIOCHEMISTRY, 1985, 24 (27) : 8005 - 8012
  • [7] 3-DIMENSIONAL STRUCTURE OF HORSE LIVER ALCOHOL-DEHYDROGENASE AT 2.4 A RESOLUTION
    EKLUND, H
    NORDSTROM, B
    ZEPPEZAUER, E
    SODERLUND, G
    OHLSSON, I
    BOIWE, T
    SODERBERG, BO
    TAPIA, O
    BRANDEN, CI
    AKESON, A
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1976, 102 (01) : 27 - &
  • [8] CRYSTALLOGRAPHIC INVESTIGATIONS OF NICOTINAMIDE ADENINE-DINUCLEOTIDE BINDING TO HORSE LIVER ALCOHOL-DEHYDROGENASE
    EKLUND, H
    SAMAMA, JP
    JONES, TA
    [J]. BIOCHEMISTRY, 1984, 23 (25) : 5982 - 5996
  • [9] Eklund H., 1987, BIOL MACROMOLECULES, V3
  • [10] ERNSTER L, 1987, CHEM SCRIPTA, V27A, P1