Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution

Rui J Sousa, Yong Je Chung, John P. Rose, Bi Cheng Wang

Research output: Contribution to journalArticle

314 Citations (Scopus)

Abstract

The crystal structure of T7 RNA polymerase reveals a molecule organized around a cleft that can accommodate a double-stranded DNA template. A portion (∼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.

Original languageEnglish (US)
Pages (from-to)593-599
Number of pages7
JournalNature
Volume364
Issue number6438
StatePublished - Aug 12 1993
Externally publishedYes

Fingerprint

Deoxyribonucleotides
Ribonucleotides
DNA Polymerase I
DNA
Catalytic Domain
RNA
Human immunodeficiency virus 1 reverse transcriptase
bacteriophage T7 RNA polymerase

ASJC Scopus subject areas

  • General

Cite this

Sousa, R. J., Chung, Y. J., Rose, J. P., & Wang, B. C. (1993). Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. Nature, 364(6438), 593-599.

Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. / Sousa, Rui J; Chung, Yong Je; Rose, John P.; Wang, Bi Cheng.

In: Nature, Vol. 364, No. 6438, 12.08.1993, p. 593-599.

Research output: Contribution to journalArticle

Sousa, RJ, Chung, YJ, Rose, JP & Wang, BC 1993, 'Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution', Nature, vol. 364, no. 6438, pp. 593-599.
Sousa RJ, Chung YJ, Rose JP, Wang BC. Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. Nature. 1993 Aug 12;364(6438):593-599.
Sousa, Rui J ; Chung, Yong Je ; Rose, John P. ; Wang, Bi Cheng. / Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. In: Nature. 1993 ; Vol. 364, No. 6438. pp. 593-599.
@article{0d6a44851f6f49f0a92dde44638aec64,
title = "Crystal structure of bacteriophage T7 RNA polymerase at 3.3 {\AA} resolution",
abstract = "The crystal structure of T7 RNA polymerase reveals a molecule organized around a cleft that can accommodate a double-stranded DNA template. A portion (∼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.",
author = "Sousa, {Rui J} and Chung, {Yong Je} and Rose, {John P.} and Wang, {Bi Cheng}",
year = "1993",
month = "8",
day = "12",
language = "English (US)",
volume = "364",
pages = "593--599",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6438",

}

TY - JOUR

T1 - Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution

AU - Sousa, Rui J

AU - Chung, Yong Je

AU - Rose, John P.

AU - Wang, Bi Cheng

PY - 1993/8/12

Y1 - 1993/8/12

N2 - The crystal structure of T7 RNA polymerase reveals a molecule organized around a cleft that can accommodate a double-stranded DNA template. A portion (∼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.

AB - The crystal structure of T7 RNA polymerase reveals a molecule organized around a cleft that can accommodate a double-stranded DNA template. A portion (∼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.

UR - http://www.scopus.com/inward/record.url?scp=0027163526&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027163526&partnerID=8YFLogxK

M3 - Article

C2 - 7688864

AN - SCOPUS:0027163526

VL - 364

SP - 593

EP - 599

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6438

ER -