REFINED CRYSTAL-STRUCTURE OF THE SERYL-TRANSFER RNA-SYNTHETASE FROM THERMUS-THERMOPHILUS AT 2-CENTER-DOT-5-ANGSTROM RESOLUTION

被引：94

作者：

FUJINAGA, M ^{[1
]}

BERTHETCOLOMINAS, C ^{[1
]}

YAREMCHUK, AD ^{[1
]}

TUKALO, MA ^{[1
]}

CUSACK, S ^{[1
]}

机构：

[1] UKRAINIAN ACAD SCI,INST MOLEC BIOL & GENET,KIEV 252627,UKRAINE

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 234卷 / 01期

关键词：

AMINOACYL-TRANSFER RNA SYNTHETASE; CRYSTAL STRUCTURE; THERMOSTABILITY; THERMUS-THERMOPHILUS; X-RAY ANALYSIS;

D O I：

10.1006/jmbi.1993.1576

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 seryl-tRNA synthetase from Thermus thermophilus has been determined and refined at, 2.5 Å resolution. The final model consists of a dimer of 421 residues each and 190 water molecules. The R-factor is 18.4% for all the data between 10 and 2.5 Å resolution. The structure is very similar to that of the homologous enzyme from Escherichia coli, with an r.m.s. difference of 1.5 Å for the 357 α-carbon atoms considered equivalent. The comparison of the two structures indicates increased hydrophobicity, reduced con formational entropy and reduced torsional strain as possible mechanisms by which thermostability is obtained in the enzyme from the thermophile.

引用

页码：222 / 233

页数：12

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