Protein Family Models

The amino terminal domain of bacteriophage lambda integrase folds into a three-stranded, antiparallel beta-sheet that packs against a C-terminal alpha-helix, adopting a fold that is structurally related to the three-stranded beta-sheet family of DNA-binding domains (which includes the GCC-box DNA-binding domain and the N-terminal domain of Tn916 integrase). This domain is responsible for high-affinity binding to each of the five DNA arm-type sites and is also a context-sensitive modulator of DNA cleavage [1]. [1]. 11904406. Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain. Wojciak JM, Sarkar D, Landy A, Clubb RT;. Proc Natl Acad Sci U S A. 2002;99:3434-3439. (from Pfam)

Date:

2024-10-16

Members of this family cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment. The catalytic site residues in CRE recombinase (Swiss:P06956) are Arg-173, His-289, Arg-292 and Tyr-324. [1]. 9082984. Flexibility in DNA recombination: structure of the lambda integrase catalytic core. Kwon HJ, Tirumalai R, Landy A, Ellenberger T;. Science 1997;276:126-131. [2]. 9288963. Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. Guo F, Gopaul DN, van Duyne GD;. Nature 1997;389:40-46. (from Pfam)

Date:

2024-10-16

tyrosine based site-specific recombinase (integrase) is involved in cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct

Date:

2022-08-22