CRYSTAL-STRUCTURE OF BACTERIOPHAGE-T7 RNA-POLYMERASE AT 3.3-ANGSTROM RESOLUTION

被引:356
|
作者
SOUSA, R
CHUNG, YJ
ROSE, JP
WANG, BC
机构
[1] UNIV PITTSBURGH,DEPT BIOL SCI,PITTSBURGH,PA 15260
[2] UNIV PITTSBURGH,DEPT CRYSTALLOG,PITTSBURGH,PA 15260
关键词
D O I
10.1038/364593a0
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
The crystal structure of T7 RNA polymerase reveals a molecule organized around a cleft that can accommodate a double-stranded DNA template. A portion (approximately 45%) of the molecule displays extensive structural homology to the polymerase domain of Klenow fragment and more limited homology to the human immunodeficiency virus HIV-1 reverse transcriptase. A comparison of the structures and sequences of these polymerases identifies structural elements that may be responsible for discriminating between ribonucleotide and deoxyribonucleotide substrates, and RNA and DNA templates. The relative locations of the catalytic site and a specific promoter recognition residue allow the orientation of the polymerase on the template to be defined.
引用
收藏
页码:593 / 599
页数:7
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