1KJK

Solution structure of the lambda integrase amino-terminal domain

Summary for 1KJK

• Entry DOI: 10.2210/pdb1kjk/pdb
• Descriptor: integrase (1 entity in total)
• Functional Keywords: dna recombination, integrase, three-stranded beta-sheet, dna-binding domain, viral protein
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 1
• Total formula weight: 7628.71

Authors

Wojciak, J.M.,Sarkar, D.,Landy, A.,Clubb, R.T. (deposition date: 2001-12-04, release date: 2002-03-27, Last modification date: 2024-05-22)

Primary citation

Wojciak, J.M.,Sarkar, D.,Landy, A.,Clubb, R.T.
Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain.
Proc.Natl.Acad.Sci.USA, 99:3434-3439, 2002

PubMed Abstract: The integrase protein (Int) from bacteriophage lambda catalyzes the insertion and excision of the viral genome into and out of Escherichia coli. It is a member of the lambda-Int family of site-specific recombinases that catalyze a diverse array of DNA rearrangements in archaebacteria, eubacteria, and yeast and belongs to the subset of this family that possesses two autonomous DNA-binding domains. The heterobivalent properties of Int can be decomposed into a carboxyl-terminal domain that executes the DNA cleavage and ligation reactions and a smaller amino-terminal domain that binds to an array of conserved DNA sites within the phage arms, thereby arranging Int protomers within the higher-order recombinogenic complex. We have determined that residues Met-1 to Leu-64 of Int constitute the minimal arm-type DNA-binding domain (INT-DBD(1-64)) and solved the solution structure by using NMR. We show that the INT-DBD(1-64) is a novel member of the growing family of three-stranded beta-sheet DNA-binding proteins, because it supplements this motif with a disordered amino-terminal basic tail that is important for arm-site binding. A model of the arm-DNA-binding domain recognizing its cognate DNA site is proposed on the basis of similarities with the analogous domain of Tn916 Int and is discussed in relation to other features of the protein.

PubMed: 11904406
DOI: 10.1073/pnas.052017999

Experimental method

SOLUTION NMR