1f44
From Proteopedia
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'''CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX''' | '''CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX''' | ||
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[[Category: Baldwin, E P.]] | [[Category: Baldwin, E P.]] | ||
[[Category: Woods, K C.]] | [[Category: Woods, K C.]] | ||
| - | [[Category: | + | [[Category: Branched dna]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Ligase/dna]] |
| - | [[Category: | + | [[Category: Protein-dna complex]] |
| - | [[Category: | + | [[Category: Recombination]] |
| - | [[Category: | + | [[Category: Site-specific recombinase]] |
| - | [[Category: | + | [[Category: Three-way junction]] |
| - | [[Category: | + | [[Category: Trimeric]] |
| - | [[Category: | + | [[Category: Y-junction]] |
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Revision as of 12:52, 2 May 2008
CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX
Overview
The crystal structure of a novel Cre-Lox synapse was solved using phases from multiple isomorphous replacement and anomalous scattering, and refined to 2.05 A resolution. In this complex, a symmetric protein trimer is bound to a Y-shaped three-way DNA junction, a marked departure from the pseudo-4-fold symmetrical tetramer associated with Cre-mediated LoxP recombination. The three-way DNA junction was accommodated by a simple kink without significant distortion of the adjoining DNA duplexes. Although the mean angle between DNA arms in the Y and X structures was similar, adjacent Cre trimer subunits rotated 29 degrees relative to those in the tetramers. This rotation was accommodated at the protein-protein and DNA-DNA interfaces by interactions that are "quasi-equivalent" to those in the tetramer, analogous to packing differences of chemically identical viral subunits at non-equivalent positions in icosahedral capsids. This structural quasi-equivalence extends to function as Cre can bind to, cleave and perform strand transfer with a three-way Lox substrate. The structure explains the dual recognition of three and four-way junctions by site-specific recombinases as being due to shared structural features between the differently branched substrates and plasticity of the protein-protein interfaces. To our knowledge, this is the first direct demonstration of quasi-equivalence in both the assembly and function of an oligomeric enzyme.
About this Structure
1F44 is a Single protein structure of sequence from Enterobacteria phage p1. Full crystallographic information is available from OCA.
Reference
Quasi-equivalence in site-specific recombinase structure and function: crystal structure and activity of trimeric Cre recombinase bound to a three-way Lox DNA junction., Woods KC, Martin SS, Chu VC, Baldwin EP, J Mol Biol. 2001 Oct 12;313(1):49-69. PMID:11601846 Page seeded by OCA on Fri May 2 15:52:24 2008
