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| - | [[Image:1f44.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1f44.png|left|200px]] |
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| | {{STRUCTURE_1f44| PDB=1f44 | SCENE= }} | | {{STRUCTURE_1f44| PDB=1f44 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX'''
| + | ===CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11601846}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11601846 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11601846}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Trimeric]] | | [[Category: Trimeric]] |
| | [[Category: Y-junction]] | | [[Category: Y-junction]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:52:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:39:11 2008'' |
Revision as of 23:39, 30 June 2008
Template:STRUCTURE 1f44
CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX
Template:ABSTRACT PUBMED 11601846
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
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