1EYV

THE CRYSTAL STRUCTURE OF NUSB FROM MYCOBACTERIUM TUBERCULOSIS

1EYV の概要

• エントリーDOI: 10.2210/pdb1eyv/pdb
• 分子名称: N-UTILIZING SUBSTANCE PROTEIN B HOMOLOG, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: helical bundle, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transcription
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33720.29

構造登録者

Gopal, B.,Haire, L.F.,Cox, R.A.,Colston, M.J.,Major, S.,Brannigan, J.A.,Smerdon, S.J.,Dodson, G.G.,TB Structural Genomics Consortium (TBSGC) (登録日: 2000-05-09, 公開日: 2000-05-18, 最終更新日: 2024-02-07)

主引用文献

Gopal, B.,Haire, L.F.,Cox, R.A.,Colston, M.J.,Major, S.,Brannigan, J.A.,Smerdon, S.J.,Dodson, G.
The crystal structure of NusB from Mycobacterium tuberculosis.
Nat.Struct.Biol., 7:475-478, 2000

PubMed Abstract: Both prokaryotes and eukaryotes regulate transcription through mechanisms that suppress termination signals. An antitermination mechanism was first characterized in bacteriophage lambda. Bacteria have analogous machinery that regulates ribosomal RNA transcription and employs host factors, called the N-utilizing (where N stands for the phage lambda N protein) substances (Nus), NusA, NusB, NusE and NusG. Here we report the crystal structure of NusB from Mycobacterium tuberculosis, the bacterium that causes tuberculosis in humans. This molecule shares a similar tertiary structure with the related Escherichia coli protein but adopts a different quaternary organization. We show that, unlike the E. coli homolog, M. tuberculosis NusB is dimeric both in solution and in the crystal. These data help provide a framework for understanding the structural and biological function of NusB in the prokaryotic transcriptional antitermination complex.

PubMed: 10881194
DOI: 10.1038/75876

実験手法

X-RAY DIFFRACTION (1.6 Å)