CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HIV-1 INTEGRASE - SIMILARITY TO OTHER POLYNUCLEOTIDYL TRANSFERASES

被引：687

作者：

DYDA, F ^{[1
]}

HICKMAN, AB ^{[1
]}

JENKINS, TM ^{[1
]}

ENGELMAN, A ^{[1
]}

CRAIGIE, R ^{[1
]}

DAVIES, DR ^{[1
]}

机构：

[1] NIDDK, MOLEC BIOL LAB, BETHESDA, MD 20892 USA

来源：

SCIENCE | 1994年 / 266卷 / 5193期

关键词：

D O I：

10.1126/science.7801124

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

HIV integrase is the enzyme responsible for inserting the viral DNA into the host chromosome; it is essential for HIV replication. The crystal structure of the catalytically active core domain (residues 50 to 212) of HIV-7 integrase was determined at 2.5 Angstrom resolution. The central feature of the structure is a five-stranded beta sheet flanked by helical regions. The overall topology reveals that this domain of integrase belongs to a superfamily of polynucleotidyl transferases that includes ribonuclease H and the Holliday junction resolvase RuvC. The active site region is identified by the position of two of the conserved carboxylate residues essential for catalysis, which are located at similar positions in ribonuclease H. In the crystal, two molecules form a dimer with an extensive solvent-inaccessible interface of 1300 Angstrom(2) per monomer.

引用

页码：1981 / 1986

页数：6

共 81 条

[41] STRUCTURAL DETAILS OF RIBONUCLEASE-H FROM ESCHERICHIA-COLI AS REFINED TO AN ATOMIC RESOLUTION [J].