Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution

被引:304
作者
Lancaster, CRD
Kröger, A
Auer, M
Michel, H
机构
[1] Max Planck Inst Biophys, D-60528 Frankfurt, Germany
[2] Goethe Univ Frankfurt, Inst Mikrobiol, D-60439 Frankfurt, Germany
关键词
D O I
10.1038/46483
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase). Here we describe the crystal structure at 2.2 Angstrom resolution of the three protein subunits containing fumarate reductase from the anaerobic bacterium Wolinella succinogenes, Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres, The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules. On the basis of the structure, we propose a pathway of electron transfer from the dihaem cytochrome b to the site of fumarate reduction and a mechanism of fumarate reduction. The relative orientations of the soluble and membrane-embedded subunits of succinate:quinone oxidoreductases appear to be unique.
引用
收藏
页码:377 / 385
页数:9
相关论文
共 50 条
  • [1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY
    BAILEY, S
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 : 760 - 763
  • [2] BIOSYNTHETIC PATHWAYS OF VIBRIO-SUCCINOGENES GROWING WITH FUMARATE AS TERMINAL ELECTRON-ACCEPTOR AND SOLE CARBON SOURCE
    BRONDER, M
    MELL, H
    STUPPERICH, E
    KROGER, A
    [J]. ARCHIVES OF MICROBIOLOGY, 1982, 131 (03) : 216 - 223
  • [3] FREE R-VALUE - A NOVEL STATISTICAL QUANTITY FOR ASSESSING THE ACCURACY OF CRYSTAL-STRUCTURES
    BRUNGER, AT
    [J]. NATURE, 1992, 355 (6359) : 472 - 475
  • [4] Crystallography & NMR system:: A new software suite for macromolecular structure determination
    Brunger, AT
    Adams, PD
    Clore, GM
    DeLano, WL
    Gros, P
    Grosse-Kunstleve, RW
    Jiang, JS
    Kuszewski, J
    Nilges, M
    Pannu, NS
    Read, RJ
    Rice, LM
    Simonson, T
    Warren, GL
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 : 905 - 921
  • [5] MOLECULAR-BIOLOGY, BIOCHEMISTRY AND BIOENERGETICS OF FUMARATE REDUCTASE, A COMPLEX MEMBRANE-BOUND IRON-SULFUR FLAVOENZYME OF ESCHERICHIA-COLI
    COLE, ST
    CONDON, C
    LEMIRE, BD
    WEINER, JH
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1985, 811 (04) : 381 - 403
  • [6] COWTAN K, 1994, JOINT CCP4 ESF EACBM, V30, P34
  • [7] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    delaFortelle, E
    Bricogne, G
    [J]. MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 : 472 - 494
  • [8] ACCURATE BOND AND ANGLE PARAMETERS FOR X-RAY PROTEIN-STRUCTURE REFINEMENT
    ENGH, RA
    HUBER, R
    [J]. ACTA CRYSTALLOGRAPHICA SECTION A, 1991, 47 : 392 - 400
  • [9] Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    Esnouf, RM
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1999, 55 : 938 - 940
  • [10] An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    Esnouf, RM
    [J]. JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 1997, 15 (02) : 132 - +