7a4h

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Aquifex aeolicus lumazine synthase-derived nucleocapsid variant NC-2 (180-mer)Aquifex aeolicus lumazine synthase-derived nucleocapsid variant NC-2 (180-mer)

Structural highlights

7a4h is a 180 chain structure with sequence from Aquifex aeolicus VF5 and Escherichia virus Lambda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 4.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

REGN_LAMBD Antitermination proteins positively regulate expression of the phage early and late gene operons. Bacterial host RNA polymerase modified by these antitermination proteins transcribes through termination sites that otherwise prevent expression of the regulated genes. N protein regulates the transition from the early to the middle stage of lytic development. It is a transcription antitermination protein that prevents termination at the rho-dependent tL and tR transcription termination sites.RISB_AQUAE Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.[1] [2]

References

  1. Haase I, Mortl S, Kohler P, Bacher A, Fischer M. Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii. Eur J Biochem. 2003 Mar;270(5):1025-32. PMID:12603336
  2. Zhang X, Meining W, Fischer M, Bacher A, Ladenstein R. X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons. J Mol Biol. 2001 Mar 9;306(5):1099-114. PMID:11237620 doi:10.1006/jmbi.2000.4435

7a4h, resolution 4.50Å

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OCA