2OXO

Crystallization and structure determination of the core-binding domain of bacteriophage lambda integrase

2OXO の概要

• エントリーDOI: 10.2210/pdb2oxo/pdb
• 分子名称: Integrase, SULFATE ION (3 entities in total)
• 機能のキーワード: dna-binding protein, four-helix bundle, dna binding protein
• 由来する生物種: unidentified phage
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11540.30

構造登録者

Kamadurai, H.B.,Jain, R.,Foster, M.P. (登録日: 2007-02-20, 公開日: 2008-02-26, 最終更新日: 2024-02-21)

主引用文献

Kamadurai, H.B.,Jain, R.,Foster, M.P.
Crystallization and structure determination of the core-binding domain of bacteriophage lambda integrase.
Acta Crystallogr.,Sect.F, 64:470-473, 2008

PubMed Abstract: Bacteriophage lambda integrase catalyzes site-specific DNA recombination. A helical bundle domain in the enzyme, called the core-binding domain (Int(CB)), promotes the catalysis of an intermediate DNA-cleavage reaction that is critical for recombination and is not well folded in solution in the absence of DNA. To gain structural insights into the mechanism behind the accessory role of this domain in catalysis, an attempt was made to crystallize an Int(CB)-DNA complex, but crystals of free Int(CB) were fortuitously obtained. The three-dimensional structure of DNA-free Int(CB) was solved at 2.0 A resolution by molecular replacement using as the search model the previously available DNA-bound 2.8 A structure of the Int(CB) domain in a larger construct of lambda integrase. The crystal structure of DNA-free Int(CB) resembles the DNA-bound structure of Int(CB), but exhibits subtle differences in the DNA-binding face and lacks electron density for ten residues in the C-terminus that form a portion of a linker connecting Int(CB) to the C-terminal catalytic domain of the enzyme. Thus, this work reveals the domain in the absence of DNA and allows comparison with the DNA-bound form of this catalytically activating domain.

PubMed: 18540053
DOI: 10.1107/S174430910801381X

実験手法

X-RAY DIFFRACTION (2 Å)