1H, 13C and 15N backbone and side chain resonance assignments of a Myxococcus xanthus anti-repressor with no known sequence homologues.
The CarS antirepressor activates a photo-inducible promoter in Myxococcus xanthus by physically interacting with the CarA repressor and eliminating the latter's binding to operator DNA. Interestingly, interactions with both CarS and operator are crucially dependent on the DNA recognition helix of the CarA winged-helix DNA-binding domain. The CarA-CarS and the CarA-operator interfaces therefore overlap, and CarS may have structural features that mimic operator DNA. CarS has no known sequence homologues and its Gly and Pro contents are unusually high. Here, we report (1)H, (13)C and (15)N backbone and side chain assignments of CarS1, an 86-residue truncated yet fully functional variant of CarS. Secondary structural elements inferred from these data differ from those predicted from sequence.
León
Esther
E
Instituto de Química Física Rocasolano, CSIC, 28006, Madrid, Spain.
González
Carlos
C
Elías-Arnanz
Montserrat
M
Padmanabhan
S
S
Jiménez
M Angeles
MA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry*
D001426:Bacterial Proteins; C091094:CarS protein, Myxococcus xanthus; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons; D014157:Transcription Factors