Linked Life Data

11601846

Source:http://linkedlifedata.com/resource/pubmed/id/11601846

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-10-16
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
313
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-69
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11601846-Attachment Sites, Microbiological, pubmed-meshheading:11601846-Base Sequence, pubmed-meshheading:11601846-Binding Sites, pubmed-meshheading:11601846-Catalysis, pubmed-meshheading:11601846-Crystallography, X-Ray, pubmed-meshheading:11601846-DNA, Bacterial, pubmed-meshheading:11601846-DNA-Binding Proteins, pubmed-meshheading:11601846-Integrases, pubmed-meshheading:11601846-Models, Molecular, pubmed-meshheading:11601846-Nucleic Acid Conformation, pubmed-meshheading:11601846-Protein Binding, pubmed-meshheading:11601846-Protein Structure, Quaternary, pubmed-meshheading:11601846-Protein Subunits, pubmed-meshheading:11601846-Recombination, Genetic, pubmed-meshheading:11601846-Rotation, pubmed-meshheading:11601846-Structure-Activity Relationship, pubmed-meshheading:11601846-Viral Proteins
pubmed:year
2001
pubmed:articleTitle
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.
pubmed:affiliation
Section of Molecular and Cellular Biology, University of California, Davis, 1 Shields Ave, Davis, CA 95616, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't