1EYV

THE CRYSTAL STRUCTURE OF NUSB FROM MYCOBACTERIUM TUBERCULOSIS

Summary for 1EYV

• Entry DOI: 10.2210/pdb1eyv/pdb
• Descriptor: N-UTILIZING SUBSTANCE PROTEIN B HOMOLOG, PHOSPHATE ION (3 entities in total)
• Functional Keywords: helical bundle, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transcription
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 33720.29

Authors

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) (deposition date: 2000-05-09, release date: 2000-05-18, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)