1EIK

Solution Structure of RNA Polymerase Subunit RPB5 from Methanobacterium Thermoautotrophicum

1EIK の概要

• エントリーDOI: 10.2210/pdb1eik/pdb
• 分子名称: RNA POLYMERASE SUBUNIT RPB5 (1 entity in total)
• 機能のキーワード: rpb5, rpbh, rna polymerase subunit, ocsp, nesg, protein structure initiative, structural genomics, psi, northeast structural genomics consortium, transferase
• 由来する生物種: Methanothermobacter thermautotrophicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8826.35

構造登録者

Yee, A.,Booth, V.,Dharamsi, A.,Engel, A.,Edwards, A.M.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (登録日: 2000-02-25, 公開日: 2000-06-21, 最終更新日: 2024-05-22)

主引用文献

Yee, A.,Booth, V.,Dharamsi, A.,Engel, A.,Edwards, A.M.,Arrowsmith, C.H.
Solution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicum.
Proc.Natl.Acad.Sci.USA, 97:6311-6315, 2000

PubMed Abstract: 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 alpha-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.

PubMed: 10841538
DOI: 10.1073/pnas.97.12.6311

実験手法

SOLUTION NMR