1drg: Difference between revisions
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|PDB= 1drg |SIZE=350|CAPTION= <scene name='initialview01'>1drg</scene>, resolution 2.55Å | |PDB= 1drg |SIZE=350|CAPTION= <scene name='initialview01'>1drg</scene>, resolution 2.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1crx|1CRX]], [[2crx|2CRX]], [[3crx|3CRX]], [[4crx|4CRX]], [[5crx|5CRX]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1drg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drg OCA], [http://www.ebi.ac.uk/pdbsum/1drg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1drg RCSB]</span> | |||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
1DRG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | 1DRG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p1 Enterobacteria phage p1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRG OCA]. | ||
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/11601846 11601846] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11601846 11601846] | ||
[[Category: Enterobacteria phage | [[Category: Enterobacteria phage p1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baldwin, E P.]] | [[Category: Baldwin, E P.]] | ||
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[[Category: trimeric]] | [[Category: trimeric]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:47:13 2008'' | ||
Revision as of 19:47, 30 March 2008
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| , resolution 2.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1CRX, 2CRX, 3CRX, 4CRX, 5CRX
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX
OverviewOverview
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 StructureAbout this Structure
1DRG is a Single protein structure of sequence from Enterobacteria phage p1. Full crystallographic information is available from OCA.
ReferenceReference
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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