Catalysis of site-specific recombination by Tn3 resolvase

被引：12
|
作者：
Olorunniji, Femi J. [1 ]
Stark, W. Marshall [1 ]
机构：
[1] Univ Glasgow, Fac Biomed & Life Sci, Glasgow G12 8QQ, Lanark, Scotland
来源：
BIOCHEMICAL SOCIETY TRANSACTIONS | 2010年 / 38卷
基金：
英国生物技术与生命科学研究理事会;
关键词：
active-site chemistry; catalytic residue; phosphoryl transfer; serine recombinase; site-specific recombination; In3; resolvase; GAMMA-DELTA-RESOLVASE; CLEAVAGE; RESIDUES;
D O I：
10.1042/BST0380417
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The active-site interactions involved in the catalysis of DNA site-specific recombination by the serine recombinases are still incompletely understood. Recent crystal structures of synaptic gamma delta resolvase-DNA intermediates and biochemical analysis of Tn3 resolvase mutants have provided new insights into the structure of the resolvase active site, and how interactions of the catalytic residues with the DNA substrate might promote the phosphoryl transfer reactions.
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页码：417 / 421
页数：5
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