1m6x: Difference between revisions
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'''Flpe-Holliday Junction Complex''' | {{Structure | ||
|PDB= 1m6x |SIZE=350|CAPTION= <scene name='initialview01'>1m6x</scene>, resolution 2.80Å | |||
|SITE= <scene name='pdbsite=CTA:Active+Catalytic+Site+Of+Monomer+A.+Y343+Is+Donated+By+M+...'>CTA</scene>, <scene name='pdbsite=CTB:Active+Catalytic+Site+Of+Monomer+B.+Y343+Is+Donated+By+M+...'>CTB</scene>, <scene name='pdbsite=CTC:Inactive+Catalytic+Site+Of+Monomer+C.+Y343+Is+Donated+By+...'>CTC</scene> and <scene name='pdbsite=CTD:Inactive+Catalytic+Site+Of+Monomer+D.+Y343+Is+Donated+By+...'>CTD</scene> | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= FLP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''Flpe-Holliday Junction Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1M6X is a [ | 1M6X is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6X OCA]. | ||
==Reference== | ==Reference== | ||
Structural plasticity of the Flp-Holliday junction complex., Conway AB, Chen Y, Rice PA, J Mol Biol. 2003 Feb 14;326(2):425-34. PMID:[http:// | Structural plasticity of the Flp-Holliday junction complex., Conway AB, Chen Y, Rice PA, J Mol Biol. 2003 Feb 14;326(2):425-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12559911 12559911] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: tyrosine recombinase]] | [[Category: tyrosine recombinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:44 2008'' | ||
Revision as of 13:39, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Sites: | , , and | ||||||
| Gene: | FLP1 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Flpe-Holliday Junction Complex
OverviewOverview
The Flp recombinase, a member of the lambda integrase or tyrosine-based family of site-specific recombinases, is an interesting example of an enzyme whose catalytic activity is regulated by protein-protein contacts. It exhibits half-of-the-sites activity throughout its catalytic cycle. Flp is unique among these recombinases, in that it assembles each active site in trans through the interaction of two protein monomers within the catalytic tetramer, with isomerization of interacting pairs being essential to complete a full reaction. We report here the structure of a DNA-bound tetramer of Flpe, a variant of Flp that is more active at 37 degrees C than the wild-type recombinase. This new structure includes the first observation of a tyrosine recombinase with an invading 5'-OH poised to attack the covalent phosphotyrosine residue. Comparison with the previously determined Flp structure highlights differences in flexibility between the two types of protein-protein interfaces in the tetramer and better defines the range of conformations available to this remarkably flexible complex. These results suggest a steric occlusion model for enforcement of half-of-the-sites activity.
About this StructureAbout this Structure
1M6X is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural plasticity of the Flp-Holliday junction complex., Conway AB, Chen Y, Rice PA, J Mol Biol. 2003 Feb 14;326(2):425-34. PMID:12559911
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