Protein Family Models

Bacteriophage P22 Cro protein represses genes normally expressed in early phage development and is necessary for the late stage of lytic growth. It does this by binding to the OL and OR operator-regions normally used by the repressor protein for lysogenic maintenance. [1]. 3954988. Bacteriophage P22 Cro protein: sequence, purification, and properties. Poteete AR, Hehir K, Sauer RT;. Biochemistry. 1986;25:251-256. [2]. 15062080. Secondary structure switching in Cro protein evolution. Newlove T, Konieczka JH, Cordes MH;. Structure. 2004;12:569-581. [3]. 18369196. N15 Cro and lambda Cro: orthologous DNA-binding domains with completely different but equally effective homodimer interfaces. Dubrava MS, Ingram WM, Roberts SA, Weichsel A, Montfort WR, Cordes MH;. Protein Sci. 2008;17:803-812. (from Pfam)

Date:

2024-10-16

This family is named for YdaS, a helix-turn-helix protein distantly related to the toxin-antitoxin system HigA antitoxin and encoded in the Rac prophage region protein in Escherichia coli K-12.

Date:

2024-10-16

This large family of DNA binding helix-turn helix proteins includes Cro Swiss:P03036 and CI Swiss:P03034. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteristic of the whole family [1]. [1]. 20196080. The crystal structure of NGO0477 from Neisseria gonorrhoeae reveals a novel protein fold incorporating a helix-turn-helix motif. Ren J, Sainsbury S, Nettleship JE, Saunders NJ, Owens RJ;. Proteins. 2010;78:1798-1802. (from Pfam)

Date:

2024-10-16

helix-turn-helix domain-containing protein binds DNA and may function as a transcriptional regulator, similar to Xylella fastidiosa Cro protein

Date:

2018-10-05