Photo CIDNP study on the complex formation of lambda cro protein with OR3.
A photo CIDNP spectrum of lambda cro repressor protein showed that one of the three tyrosines and His 35 are quite accessible to the photosensitive dye. For the remaining two tyrosine residues one is slightly accessible, but the other is inaccessible. In comparison with the result of differential nitration at tyrosine side chains followed by the peptide analysis, it can be concluded that Tyr 26 is mostly exposed and Tyr 51 is slightly exposed on the surface of the cro dimer. On the addition of OR3 17mer, His 35 and Tyr 26 are no longer accessible to the dye, which indicates that they are involved in interaction. However, a similar phenomenon was observed by adding CAP binding site 22mer. The interaction mechanism will be discussed.
Shirakawa
M
M
Lee
S J
SJ
Akutsu
H
H
Kyogoku
Y
Y
Kitano
K
K
Shin
M
M
Ohtsuka
E
E
Ikehara
M
M
D010582:Bacteriophage lambda / Q000235:genetics*; D004268:DNA-Binding Proteins; D005814:Genes, Viral; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D009876:Operon; D012097:Repressor Proteins / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D014443:Tyrosine; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins
D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins; D014443:Tyrosine