Crystals of Thermus thermophilus tRNA Asp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%.: Comparison with other aminoacylation systems

被引：4

作者：

Briand, C ^{[1
]}

Poterszman, A ^{[1
]}

Mitschler, A ^{[1
]}

Yusupov, M ^{[1
]}

Thierry, JC ^{[1
]}

Moras, D ^{[1
]}

机构：

[1] ULP, INSERM, CNRS, IGBMC,Lab Biol Struct,UPR 9004, F-67404 Illkirch Graffenstaden, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1998年 / 54卷

关键词：

D O I：

10.1107/S0907444998005800

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Thermus thermophilus tRNA(Asp), purified from a nonrecombinant source, has been crystallized ina-complex with its cognate dimeric (alpha 2) aspartyl-tRNA synthetase. Crystals diffract to 2.9 Angstrom resolution and belong to space group P6(3) with cell parameters a = b = 258, c = 90.9 Angstrom. The crystals contain one aspartyl-tRNA synthetase dimer and two tRNA molecules in the asymmetric unit, corresponding to a V-m of 4.85 Angstrom Da(-1) and 75% solvent content, When compared with those obtained for globular proteins these values are high, but fall within the range observed for other aminoacyl-tRNA Synthetases, either free or complexed with their tRNAs. A comparative survey is presented here.

引用

页码：1382 / 1386

页数：5

共 41 条

[1] Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase [J].

Aberg, A ;

Yaremchuk, A ;

Tukalo, M ;

Rasmussen, B ;

Cusack, S .

BIOCHEMISTRY, 1997, 36 (11) :3084-3094

[2] CRYSTAL-STRUCTURE OF HISTIDYL-TRANSFER-RNA SYNTHETASE FROM ESCHERICHIA-COLI COMPLEXED WITH HISTIDYL-ADENYLATE [J].

ARNEZ, JG ;

HARRIS, DC ;

MITSCHLER, A ;

REES, B ;

FRANCKLYN, CS ;

MORAS, D .

EMBO JOURNAL, 1995, 14 (17) :4143-4155

[3] Structural and functional considerations of the aminoacylation reaction [J].

Arnez, JG ;

Moras, D .

TRENDS IN BIOCHEMICAL SCIENCES, 1997, 22 (06) :211-216

[4] CRYSTAL-STRUCTURES AT 2.5 ANGSTROM RESOLUTION OF SERYL-TRANSFER-RNA SYNTHETASE COMPLEXED 2 ANALOGS OF SERYL ADENYLATE [J].

BELRHALI, H ;

YAREMCHUK, A ;

TUKALO, M ;

LARSEN, K ;

BERTHETCOLOMINAS, C ;

LEBERMAN, R ;

BEIJER, B ;

SPROAT, B ;

ALSNIELSEN, J ;

GRUBEL, G ;

LEGRAND, JF ;

LEHMANN, M ;

CUSACK, S .

SCIENCE, 1994, 263 (5152) :1432-1436

[5] Crystallization of Escherichia coli aspartyl-tRNA synthetase in its free state and in a complex with yeast tRNA(Asp) [J].

Boeglin, M ;

DockBregeon, AC ;

Eriani, G ;

Gangloff, J ;

Ruff, M ;

Poterszman, A ;

Mitschler, A ;

Thierry, JC ;

Moras, D .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1996, 52 :211-214

[6] STRUCTURE OF TYROSYL TRANSFER-RNA SYNTHETASE REFINED AT 2.3-A RESOLUTION - INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE [J].

BRICK, P ;

BHAT, TN ;

BLOW, DM .

JOURNAL OF MOLECULAR BIOLOGY, 1989, 208 (01) :83-98

[7] CRYSTALLOGRAPHIC STUDY AT 2.5A RESOLUTION OF THE INTERACTION OF METHIONYL-TRANSFER-RNA SYNTHETASE FROM ESCHERICHIA-COLI WITH ATP [J].

BRUNIE, S ;

ZELWER, C ;

RISLER, JL .

JOURNAL OF MOLECULAR BIOLOGY, 1990, 216 (02) :411-424

[8]

CARTER CW, 1979, J BIOL CHEM, V254, P2219

[9] THE ACTIVE-SITE OF YEAST ASPARTYL-TRANSFER-RNA SYNTHETASE - STRUCTURAL AND FUNCTIONAL-ASPECTS OF THE AMINOACYLATION REACTION [J].

CAVARELLI, J ;

ERIANI, G ;

REES, B ;

RUFF, M ;

BOEGLIN, M ;

MITSCHLER, A ;

MARTIN, F ;

GANGLOFF, J ;

THIERRY, JC ;

MORAS, D .

EMBO JOURNAL, 1994, 13 (02) :327-337

[10] CRYSTALLIZATION OF THREONYL-TRANSFER-RNA SYNTHETASE FROM THERMUS-THERMOPHILUS AND PRELIMINARY CRYSTALLOGRAPHIC DATA [J].

CURA, V ;

KERN, D ;

MITSCHLER, A ;

MORAS, D .

FEBS LETTERS, 1995, 374 (01) :110-112

← 1 2 3 4 5 →