Difference between revisions of "MtrB"

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=References=
 
=References=
  
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<pubmed>7715723 10499579 11566976 7515880, </pubmed>
 
# Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P (1995) The structure of ''trp'' RNA-binding protein. Nature 374:693-700. [http://www.ncbi.nlm.nih.gov/sites/entrez/7715723 PubMed]
 
# Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P (1995) The structure of ''trp'' RNA-binding protein. Nature 374:693-700. [http://www.ncbi.nlm.nih.gov/sites/entrez/7715723 PubMed]
 
# Antson AA, Dodson EJ, Dodson G, Greaves RB, Chen XP, Gollnick P (1999) Structure of the ''trp'' RNA-binding attenuation protein, TRAP, bound to RNA. Nature 401:235-242. [http://www.ncbi.nlm.nih.gov/sites/entrez/10499579 PubMed]
 
# Antson AA, Dodson EJ, Dodson G, Greaves RB, Chen XP, Gollnick P (1999) Structure of the ''trp'' RNA-binding attenuation protein, TRAP, bound to RNA. Nature 401:235-242. [http://www.ncbi.nlm.nih.gov/sites/entrez/10499579 PubMed]

Revision as of 20:12, 8 June 2009

  • Description: tryptophan operon RNA-binding attenuation protein (TRAP)

Gene name mtrB
Synonyms
Essential no
Product tryptophan operon RNA-binding attenuation protein (TRAP)
Function regulation of tryptophan biosynthesis

(and translation) attenuation in the trp operon); repression of the folate operon

MW, pI 8 kDa, 7.333
Gene length, protein length 225 bp, 75 aa
Immediate neighbours hepS, mtrA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MtrB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU22770

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: prpD family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Structure: 2ZD0 (mutant TRAP, Geobacillus stearothermophilus), 1WAP (complex with L-tryptophan)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

  1. Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P (1995) The structure of trp RNA-binding protein. Nature 374:693-700. PubMed
  2. Antson AA, Dodson EJ, Dodson G, Greaves RB, Chen XP, Gollnick P (1999) Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. Nature 401:235-242. PubMed
  3. Babitzke P, Gollnick P (2001) Posttransription iniation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure. J Bacteriol 183:5795-5802. PubMed
  4. Babitzke P, Stults JT, Shire SJ, Yanofsky C (1994) TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts. J Biol Chem 269:16597-16604. PubMed
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed