3-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE - INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA-COLI REFINED AT 2.0-A RESOLUTION

被引:94
作者
WILMANNS, M
PRIESTLE, JP
NIERMANN, T
JANSONIUS, JN
机构
[1] UNIV BASEL, BIOCTR, DEPT STRUCT BIOL, CH-4056 BASEL, SWITZERLAND
[2] UNIV BASEL, BIOCTR, DEPT BIOPHYS CHEM, CH-4056 BASEL, SWITZERLAND
关键词
BETA-ALPHA-BARREL; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; CRYSTAL STRUCTURE; BIFUNCTIONAL ENZYME;
D O I
10.1016/0022-2836(92)90665-7
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 three-dimensional structure of the monomeric bifunctional enzyme N-(5′-phosphoribosyl)anthranilate isomerase: indole-3-glycerol-phosphate synthase from Escherichia coli has been refined at 2·0 Å resolution, using oscillation film data obtained from synchrotron radiation. The model includes the complete protein (452 residues), two phosphate ions and 628 water molecules. The final R-factor is 17·3% for all observed data between 15 and 2 Å resolution. The root-mean-square deviations from ideal bond lengths and bond angles are 0·010 Å and 3·2 °, respectively. The structure of N-(5′-phosphoribosyl)anthranilate isomerase: indole-3-glycerol-phosphate synthase from E. coli comprises two β α-barrel domains that superimpose with a root-mean-square deviation of 2·03 Å for 138 Cα-pairs. The C-terminal domain (residues 256 to 452) catalyses the PRAI reaction and the N-terminal domain (residues 1 to 255) catalyses the IGPS reaction, two sequential steps in tryptophan biosynthesis. The enzyme has the overall shape of a dumb-bell, resulting in a surface area that is considerably larger than normally observed for monomeric proteins of this size. The active sites of the PRAI and the IGPS domains, both located at the C-terminal side of the central β-barrel, contain equivalent binding sites for the phosphate moieties of the substrates N-(5′-phosphoribosyl) anthranilate and 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate. These two phosphate binding sites are identical with respect to their positions within the tertiary structure of the β α-barrel, the conformation of the residues involved in phosphate binding and the hydrogen-bonding network between the phosphate ions and the protein. The active site cavities of both domains contain similar hydrophobic pockets that presumably bind the anthranilic acid moieties of the substrates. These similarities of the tertiary structures and the active sites of the two domains provide evidence that N-(5′-phosphoribosyl)anthranilate isomerase: indole-3-glycerol-phosphate synthase from E. coli results from a gene duplication event of a monomeric β α-barrel ancestor. © 1992.
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页码:477 / 507
页数:31
相关论文
共 71 条
  • [1] STRUCTURE OF CHICKEN MUSCLE TRIOSE PHOSPHATE ISOMERASE DETERMINED CRYSTALLOGRAPHICALLY AT 2.5A RESOLUTION USING AMINO-ACID SEQUENCE DATA
    BANNER, DW
    BLOOMER, AC
    PETSKO, GA
    PHILLIPS, DC
    POGSON, CI
    WILSON, IA
    CORRAN, PH
    FURTH, AJ
    MILMAN, JD
    OFFORD, RE
    PRIDDLE, JD
    WALEY, SG
    [J]. NATURE, 1975, 255 (5510) : 609 - 614
  • [2] CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING - APPLICATION TO CRAMBIN
    BRUNGER, AT
    KARPLUS, M
    PETSKO, GA
    [J]. ACTA CRYSTALLOGRAPHICA SECTION A, 1989, 45 : 50 - 61
  • [3] CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING APPLICATION TO A 2.8-A RESOLUTION STRUCTURE OF ASPARTATE-AMINOTRANSFERASE
    BRUNGER, AT
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1988, 203 (03) : 803 - 816
  • [4] CRYSTALLOGRAPHIC R-FACTOR REFINEMENT BY MOLECULAR-DYNAMICS
    BRUNGER, AT
    KURIYAN, J
    KARPLUS, M
    [J]. SCIENCE, 1987, 235 (4787) : 458 - 460
  • [5] GENE STRUCTURE IN THE TRYPTOPHAN OPERON OF ESCHERICHIA-COLI - NUCLEOTIDE-SEQUENCE OF TRPC AND THE FLANKING INTERCISTRONIC REGIONS
    CHRISTIE, GE
    PLATT, T
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1980, 142 (04) : 519 - 530
  • [6] N-(5-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE-INDOLEGLYCEROL-PHOSPHATE SYNTHASE .2. FAST-REACTION STUDIES SHOW THAT A FLUORESCENT SUBSTRATE-ANALOG BINDS INDEPENDENTLY TO 2 DIFFERENT SITES
    COHN, W
    KIRSCHNER, K
    PAUL, C
    [J]. BIOCHEMISTRY, 1979, 18 (26) : 5953 - 5959
  • [7] SOLVENT-ACCESSIBLE SURFACES OF PROTEINS AND NUCLEIC-ACIDS
    CONNOLLY, ML
    [J]. SCIENCE, 1983, 221 (4612) : 709 - 713
  • [8] FUNCTIONAL EVOLUTIONARY DIVERGENCE OF PROTEOLYTIC-ENZYMES AND THEIR INHIBITORS
    CREIGHTON, TE
    DARBY, NJ
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1989, 14 (08) : 319 - 324
  • [9] MODIFICATION OF A CATALYTICALLY IMPORTANT RESIDUE OF INDOLEGLYCEROL-PHOSPHATE SYNTHASE FROM ESCHERICHIA-COLI
    EBERHARD, M
    KIRSCHNER, K
    [J]. FEBS LETTERS, 1989, 245 (1-2): : 219 - 222
  • [10] DNA-SEQUENCES AND CHARACTERIZATION OF 4 EARLY GENES OF THE TRYPTOPHAN PATHWAY IN PSEUDOMONAS-AERUGINOSA
    ESSAR, DW
    EBERLY, L
    HAN, CY
    CRAWFORD, IP
    [J]. JOURNAL OF BACTERIOLOGY, 1990, 172 (02) : 853 - 866