Solution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicum

被引：17

作者：

Yee, A

Booth, V

Dharamsi, A

Engel, A

Edwards, AM

Arrowsmith, CH

机构：

[1] Univ Toronto, Ontario Canc Inst, Div Mol & Struct Biol, Toronto, ON M5G 2M9, Canada

[2] Univ Toronto, Dept Med Biophys, Toronto, ON M5G 2M9, Canada

[3] Univ Toronto, Banting & Best Dept Med Res, Charles H Best Inst, Toronto, ON M5G 1L6, Canada

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2000年 / 97卷 / 12期

关键词：

D O I：

10.1073/pnas.97.12.6311

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：

RPB5 is an essential subunit of eukaryotic and archaeal RNA polymerases. It is a proposed target for transcription activator proteins in eukaryotes, but the mechanism of interaction is not known. We have determined the solution structure of the RPB5 subunit from the thermophilic archeon, Methanobacterium thermoautotrophicum. MtRBP5 contains a four-stranded beta-sheet platform supporting two rw-helices, one on each side of the beta-sheet, resulting in an overall mushroom shape that does not appear to have any structural homologues in the structural database. The position and conservation of charged surface residues suggests possible modes of interaction with other proteins, as well as a rationale for the thermal stability of this protein.

引用

页码：6311 / 6315

页数：5

共 34 条

[1] CLONING AND SEQUENCE DETERMINATION OF THE SCHIZOSACCHAROMYCES-POMBE RPB1 GENE ENCODING THE LARGEST SUBUNIT OF RNA POLYMERASE-II [J].