PDBsum entry 1eyv

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Transcription PDB id
Protein chains
131 a.a. *
PO4 ×2
Waters ×291
* Residue conservation analysis
PDB id:
Name: Transcription
Title: The crystal structure of nusb from mycobacterium tuberculosis
Structure: N-utilizing substance protein b homolog. Chain: a, b. Synonym: nusb protein. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
1.60Å     R-factor:   0.190     R-free:   0.234
Authors: B.Gopal,L.F.Haire,R.A.Cox,M.J.Colston,S.Major,J.A.Brannigan, S.J.Smerdon,G.G.Dodson,Tb Structural Genomics Consortium (Tbsgc)
Key ref:
B.Gopal et al. (2000). The crystal structure of NusB from Mycobacterium tuberculosis. Nat Struct Biol, 7, 475-478. PubMed id: 10881194 DOI: 10.1038/75876
09-May-00     Release date:   18-May-00    
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Protein chains
P9WIV1  (NUSB_MYCTU) -  N utilization substance protein B homolog
156 a.a.
131 a.a.
Key:    Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     transcription, DNA-dependent   3 terms 
  Biochemical function     RNA binding     1 term  


DOI no: 10.1038/75876 Nat Struct Biol 7:475-478 (2000)
PubMed id: 10881194  
The crystal structure of NusB from Mycobacterium tuberculosis.
B.Gopal, L.F.Haire, R.A.Cox, M.Jo Colston, S.Major, J.A.Brannigan, S.J.Smerdon, G.Dodson.
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.
  Selected figure(s)  
Figure 1.
Figure 1. Stereo view of the monomer of NusB. The seven -helices (A -G) in this C trace pack to form a wedge-shaped molecule with overall dimensions of 25 30 45 . Every 10^th residue is numbered.
Figure 4.
Figure 4. Sequence and structural comparison between NusB homologs. a, The consensus secondary structure is shown under the sequences. b, Location of the conserved residues in NusB. The conserved residues mostly comprise the core of the molecule, implying that most NusB homologs have a similar structure.
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 475-478) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18757535 K.B.Arnvig, S.Zeng, S.Quan, A.Papageorge, N.Zhang, A.C.Villapakkam, and C.L.Squires (2008).
Evolutionary comparison of ribosomal operon antitermination function.
  J Bacteriol, 190, 7251-7257.  
18177898 R.Das, S.Loss, J.Li, D.S.Waugh, S.Tarasov, P.T.Wingfield, R.A.Byrd, and A.S.Altieri (2008).
Structural biophysics of the NusB:NusE antitermination complex.
  J Mol Biol, 376, 705-720.
PDB code: 2jr0
19111659 X.Luo, H.H.Hsiao, M.Bubunenko, G.Weber, D.L.Court, M.E.Gottesman, H.Urlaub, and M.C.Wahl (2008).
Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.
  Mol Cell, 32, 791-802.
PDB codes: 3d3b 3d3c
15146506 J.Liu, H.Yokota, R.Kim, and S.H.Kim (2004).
A conserved hypothetical protein from Mycoplasma genitalium shows structural homology to nusb proteins.
  Proteins, 55, 1082-1086.
PDB code: 1q8c
12915092 M.Bellinzoni, and G.Riccardi (2003).
Techniques and applications: The heterologous expression of Mycobacterium tuberculosis genes is an uphill road.
  Trends Microbiol, 11, 351-358.  
14656444 P.G.Foster, C.R.Nunes, P.Greene, D.Moustakas, and R.M.Stroud (2003).
The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate.
  Structure, 11, 1609-1620.
PDB codes: 1sqf 1sqg
12198166 T.Steiner, J.T.Kaiser, S.Marinkoviç, R.Huber, and M.C.Wahl (2002).
Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities.
  EMBO J, 21, 4641-4653.
PDB codes: 1m1g 1m1h
11170413 B.Gopal, K.G.Papavinasasundaram, G.Dodson, M.J.Colston, S.A.Major, and A.N.Lane (2001).
Spectroscopic and thermodynamic characterization of the transcription antitermination factor NusE and its interaction with NusB from Mycobacterium tuberculosis.
  Biochemistry, 40, 920-928.  
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