A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels

被引:23
作者
Ammelburg, Moritz [1 ]
Hartmann, Marcus D. [1 ]
Djuranovic, Sergej [1 ]
Alva, Vikrarn [1 ]
Koretke, Kristin K. [2 ]
Martin, Joerg [1 ]
Sauer, Guido [3 ]
Truffault, Vincent [1 ]
Zeth, Kornelius [1 ]
Lupas, Andrei N. [1 ]
Coles, Murray [1 ]
机构
[1] Max Planck Inst Dev Biol, Dept Protein Evolut, D-72076 Tubingen, Germany
[2] GalxoSmithKlin, Computat Chem Grp, Collegeville, PA 19426 USA
[3] Max Planck Inst Dev Biol, Dept Biochem, D-72076 Tubingen, Germany
关键词
D O I
10.1016/j.str.2007.09.027
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
Proteins of the cradle-loop barrel metafold are formed by duplication of a conserved beta alpha beta-element, suggesting a common evolutionary origin from an ancestral group of nucleic acid-binding proteins. The basal fold within this metafold, the RIFT barrel, is also found in a wide range of enzymes, whose homologous relationship with the nucleic acid-binding group is unclear. We have characterized a protein family that is intermediate in sequence and structure between the basal group of cradle-loop barrels and one family of RIFT-barrel enzymes, the riboflavin kinases. We report the structure, substrate-binding mode, and catalytic activity for one of these proteins, Methanocaldococcus jannaschii Mj0056, which is an archaeal riboflavin kinase. Mj0056 is unusual in utilizing CTP rather than ATP as the donor nucleotide, and sequence conservation in the relevant residues suggests that this is a general feature of archaeal riboflavin kinases.
引用
收藏
页码:1577 / 1590
页数:14
相关论文
共 26 条
  • [1] Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold
    Bauer, S
    Kemter, K
    Bacher, A
    Huber, R
    Fischer, M
    Steinbacher, S
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2003, 326 (05) : 1463 - 1473
  • [2] A comprehensive update of the sequence and structure classification of kinases
    Cheek, S
    Ginalski, K
    Zhang, H
    Grishin, NV
    [J]. BMC STRUCTURAL BIOLOGY, 2005, 5
  • [3] COLEMAN K, 1999, ISOLATION PURIFICATI, V3, P9
  • [4] AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi β barrels
    Coles, M
    Djuranovic, S
    Söding, J
    Frickey, T
    Koretke, K
    Truffault, V
    Martin, J
    Lupas, AN
    [J]. STRUCTURE, 2005, 13 (06) : 919 - 928
  • [5] Common evolutionary origin of swapped-hairpin and double-psi β barrels
    Coles, Murray
    Hulko, Michael
    Djuranovic, Sergej
    Truffault, Vincent
    Koretke, Kristin
    Martin, Joerg
    Lupas, Andrei N.
    [J]. STRUCTURE, 2006, 14 (10) : 1489 - 1498
  • [6] Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    Cornilescu, G
    Delaglio, F
    Bax, A
    [J]. JOURNAL OF BIOMOLECULAR NMR, 1999, 13 (03) : 289 - 302
  • [7] An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments
    Diercks, T
    Coles, M
    Kessler, H
    [J]. JOURNAL OF BIOMOLECULAR NMR, 1999, 15 (02) : 177 - 180
  • [8] Extended flip-back schemes for sensitivity enhancement in multidimensional HSQC-type out-and-back experiments
    Diercks, T
    Daniels, M
    Kaptein, R
    [J]. JOURNAL OF BIOMOLECULAR NMR, 2005, 33 (04) : 243 - 259
  • [9] Coot:: model-building tools for molecular graphics
    Emsley, P
    Cowtan, K
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 : 2126 - 2132
  • [10] PROTEIN-STRUCTURE COMPARISON BY ALIGNMENT OF DISTANCE MATRICES
    HOLM, L
    SANDER, C
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1993, 233 (01) : 123 - 138