Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli

被引:10
作者
Bader, G
Gomez-Ortiz, M
Haussmann, C
Bacher, A
Huber, R
Fischer, M
机构
[1] Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany
[2] Tech Univ Munich, Lehrstuhl Organ Chem & Biochem, D-85747 Garching, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷
关键词
D O I
10.1107/S0907444904007164
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The moaABC operon of Escherichia coli is involved in early steps of the biosynthesis of the molybdenum-binding cofactor molybdopterin, but the precise functions of the cognate proteins are not known. The crystal structure of the MoaB protein from E. coli was determined by multiple anomalous dispersion at 2.1 Angstrom resolution and refined to an R factor of 20.4% (R-free = 25.0%). The protein is a 32-symmetric hexamer, with the monomers consisting of a central beta-sheet flanked by helices on both sides. The overall fold of the monomer is similar to those of the MogA protein of E. coli, the G-domains of rat and human gephyrin and the G-domains of Cnx1 protein from A. thaliana, all of which are involved in the insertion of an unknown molybdenum species into molybdopterin to form the molybdenum cofactor. Furthermore, the MoaB protein shows significant sequence similarity to the cinnamon protein from Drosophila melanogaster. In addition to other functions, all these proteins are involved in the biosynthesis of the molybdenum cofactor and have been shown to bind molybdopterin. The close structural homology to MogA and the gephyrin and Cnx1 domains suggests that MoaB may bind a hitherto unidentified pterin compound, possibly an intermediate in molybdopterin biosynthesis.
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页码:1068 / 1075
页数:8
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共 52 条
[1]   Methods used in the structure determination of bovine mitochondrial F-1 ATPase [J].
Abrahams, JP ;
Leslie, AGW .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1996, 52 :30-42
[2]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[3]   ALSCRIPT - A TOOL TO FORMAT MULTIPLE SEQUENCE ALIGNMENTS [J].
BARTON, GJ .
PROTEIN ENGINEERING, 1993, 6 (01) :37-40
[4]   Divergence in macromolecular assembly:: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus [J].
Braden, BC ;
Velikovsky, CA ;
Cauerhff, AA ;
Polikarpov, I ;
Goldbaum, FA .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 297 (05) :1031-1036
[5]  
Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254
[6]  
BULLOCK WO, 1987, BIOTECHNIQUES, V5, P376
[7]   STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE [J].
CHAN, MK ;
MUKUND, S ;
KLETZIN, A ;
ADAMS, MWW ;
REES, DC .
SCIENCE, 1995, 267 (5203) :1463-1469
[8]   Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods [J].
delaFortelle, E ;
Bricogne, G .
MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :472-494
[9]   The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein [J].
Eaves, DJ ;
Palmer, T ;
Boxer, DH .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 246 (03) :690-697
[10]   Postsynaptic clustering of major GABAA receptor subtypes requires the γ2 subunit and gephyrin [J].
Essrich, C ;
Lorez, M ;
Benson, JA ;
Fritschy, JM ;
Lüscher, B .
NATURE NEUROSCIENCE, 1998, 1 (07) :563-571