Nucleic acid recognition by OB-fold proteins

被引:392
作者
Theobald, DL [1 ]
Mitton-Fry, RM [1 ]
Wuttke, DS [1 ]
机构
[1] Univ Colorado, Dept Chem & Biochem, Boulder, CO 80309 USA
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 2003年 / 32卷
关键词
single stranded; protein fold; structural alignment;
D O I
10.1146/annurev.biophys.32.110601.142506
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 OB-fold domain is a compact structural motif frequently used for nucleic acid recognition. Structural comparison of all OB-fold/nucleic acid complexes solved to date confirms the low degree of sequence similarity among members of this family while highlighting several structural sequence determinants common to most of these OB-folds. Loops connecting the secondary structural elements in the OB-fold core are extremely variable in length and in functional detail. However, certain features of ligand binding are conserved among OB-fold complexes, including the location of the binding surface, the polarity of the nucleic acid with respect to the OB-fold, and particular nucleic acid-protein interactions commonly used for recognition of single-stranded and unusually structured nucleic acids. Intriguingly, the observation of shared nucleic acid polarity may shed light on the longstanding question concerning OB-fold origins, indicating that it is unlikely that members of this family arose vi a convergent evolution.
引用
收藏
页码:115 / 133
页数:27
相关论文
共 80 条
  • [21] Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein α subunit both uncomplexed and complexed with telomeric ssDNA
    Classen, S
    Ruggles, JA
    Schultz, SC
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2001, 314 (05) : 1113 - 1125
  • [22] SOLUTION STRUCTURE OF THE ANTICODON-BINDING DOMAIN OF ESCHERICHIA-COLI LYSYL-TRANSFER-RNA SYNTHETASE AND STUDIES OF ITS INTERACTION WITH TRNA(LYS)
    COMMANS, S
    PLATEAU, P
    BLANQUET, S
    DARDEL, F
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1995, 253 (01) : 100 - 113
  • [23] Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer
    Diedrich, G
    Spahn, CMT
    Stelzl, U
    Schäfer, MA
    Wooten, T
    Bochkariov, DE
    Cooperman, BS
    Traut, RR
    Nierhaus, KH
    [J]. EMBO JOURNAL, 2000, 19 (19) : 5241 - 5250
  • [24] DOLAN JW, 1990, J BIOL CHEM, V265, P5747
  • [26] ATTACHMENT SITES OF PRIMARY BINDING PROTEIN-L1, PROTEIN-L2 AND PROTEIN-L23 ON 23-S RIBOSOMAL-RNA OF ESCHERICHIA-COLI
    EGEBJERG, J
    CHRISTIANSEN, J
    GARRETT, RA
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1991, 222 (02) : 251 - 264
  • [27] Synthesis of aspartyl-tRNAAsp in Escherichia coli -: a snapshot of the second step
    Eiler, S
    Dock-Bregeon, AC
    Moulinier, L
    Thierry, JC
    Moras, D
    [J]. EMBO JOURNAL, 1999, 18 (22) : 6532 - 6541
  • [28] Est1 and Cdc13 as comediators of telomerase access
    Evans, SK
    Lundblad, V
    [J]. SCIENCE, 1999, 286 (5437) : 117 - 120
  • [29] Modulation of telomerase activity by telomere DNA-binding proteins in Oxytricha
    Froelich-Ammon, SJ
    Dickinson, BA
    Bevilacqua, JM
    Schultz, SC
    Cech, TR
    [J]. GENES & DEVELOPMENT, 1998, 12 (10) : 1504 - 1514
  • [30] GARVIK B, 1995, MOL CELL BIOL, V15, P6128