1HQM

CRYSTAL STRUCTURE OF THERMUS AQUATICUS CORE RNA POLYMERASE-INCLUDES COMPLETE STRUCTURE WITH SIDE-CHAINS (EXCEPT FOR DISORDERED REGIONS)-FURTHER REFINED FROM ORIGINAL DEPOSITION-CONTAINS ADDITIONAL SEQUENCE INFORMATION

「1DDQ」から置き換えられました

1HQM の概要

• エントリーDOI: 10.2210/pdb1hqm/pdb
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (6 entities in total)
• 機能のキーワード: transferase, dna-directed rna polymerase
• 由来する生物種: Thermus aquaticus; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 347937.78

構造登録者

Minakhin, L.,Bhagat, S.,Brunning, A.,Campbell, E.A.,Darst, S.A.,Ebright, R.H.,Severinov, K. (登録日: 2000-12-18, 公開日: 2001-02-07, 最終更新日: 2024-02-07)

主引用文献

Minakhin, L.,Bhagat, S.,Brunning, A.,Campbell, E.A.,Darst, S.A.,Ebright, R.H.,Severinov, K.
Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly.
Proc.Natl.Acad.Sci.USA, 98:892-897, 2001

PubMed Abstract: Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We show that omega is homologous in sequence and structure to RPB6, an essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia coli, overproduction of omega suppresses the assembly defect caused by substitution of residue 1362 of the largest subunit of RNAP, beta'. In yeast, overproduction of RPB6 suppresses the assembly defect caused by the equivalent substitution in the largest subunit of RNAP II, RPB1. High-resolution structural analysis of the omega-beta' interface in bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP II, confirms the structural relationship and suggests a "latching" mechanism for the role of omega and RPB6 in promoting RNAP assembly.

PubMed: 11158566
DOI: 10.1073/pnas.98.3.892

実験手法

X-RAY DIFFRACTION (3.3 Å)