Domain-domain communication in aminoacyl-tRNA synthetases

被引：42
作者：
Alexander, RW [1 ]
Schimmel, P
机构：
[1] Wake Forest Univ, Dept Chem, Winston Salem, NC 27109 USA
[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
来源：
PROGRESS IN NUCLEIC ACID RESEARCH AND MOLECULAR BIOLOGY, VOL 69 | 2001年 / 69卷
关键词：
D O I：
10.1016/S0079-6603(01)69050-0
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：
引用
收藏
页码：317 / 349
页数：33
相关论文
共 134 条
[1]   Evidence for breaking domain-domain functional communication in a synthetase-tRNA complex [J].
Alexander, RW ;
Schimmel, P .
BIOCHEMISTRY, 1999, 38 (49) :16359-16365
[2]   Activation of microhelix charging by localized helix destabilization [J].
Alexander, RW ;
Nordin, BE ;
Schimmel, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (21) :12214-12219
[3]  
[Anonymous], 1974, ENZYMES
[4]   Structural and functional considerations of the aminoacylation reaction [J].
Arnez, JG ;
Moras, D .
TRENDS IN BIOCHEMICAL SCIENCES, 1997, 22 (06) :211-216
[5]   Vibrational dynamics of transfer RNAs: Comparison of the free and synthetase-bound forms [J].
Bahar, I ;
Jernigan, RL .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 281 (05) :871-884
[6]  
BALDWIN AN, 1966, J BIOL CHEM, V241, P839
[7]   THE STRUCTURAL BASIS FOR SERYL-ADENYLATE AND AP(4)A SYNTHESIS BY SERYL-TRANSFER-RNA SYNTHETASE [J].
BELRHALI, H ;
YAREMCHUK, A ;
TUKALO, M ;
BERTHETCOLOMINAS, C ;
RASMUSSEN, B ;
BOSECKE, P ;
DIAT, O ;
CUSACK, S .
STRUCTURE, 1995, 3 (04) :341-352
[8]  
Beuning PJ, 1999, BIOPOLYMERS, V52, P1
[9]   THE 2.9 ANGSTROM CRYSTAL-STRUCTURE OF THERMUS-THERMOPHILUS SERYL-TRANSFER-RNA SYNTHETASE COMPLEXED WITH TRNA(SER) [J].
BIOU, V ;
YAREMCHUK, A ;
TUKALO, M ;
CUSACK, S .
SCIENCE, 1994, 263 (5152) :1404-1410
[10]   MECHANISM OF ACTION OF METHIONYL-TRANSFER RNA-SYNTHETASE FROM ESCHERICHIA-COLI .1. FLUORESCENCE STUDIES ON TRANSFER RNA MET BINDING AS A FUNCTION OF LIGANDS, IONS AND PH [J].
BLANQUET, S ;
IWATSUBO, M ;
WALLER, J .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1973, 36 (01) :213-226
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