1flo
From Proteopedia
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|PDB= 1flo |SIZE=350|CAPTION= <scene name='initialview01'>1flo</scene>, resolution 2.65Å | |PDB= 1flo |SIZE=350|CAPTION= <scene name='initialview01'>1flo</scene>, resolution 2.65Å | ||
|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>, <scene name='pdbsite=CTD:Inactive+Catalytic+Site+Of+Monomer+D.+Y343+Is+Donated+By+...'>CTD</scene> and <scene name='pdbsite=PHO:Scissle+Phosphates'>PHO</scene> | |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>, <scene name='pdbsite=CTD:Inactive+Catalytic+Site+Of+Monomer+D.+Y343+Is+Donated+By+...'>CTD</scene> and <scene name='pdbsite=PHO:Scissle+Phosphates'>PHO</scene> | ||
- | |LIGAND= <scene name='pdbligand=PHS:PHOSPHONIC ACID'>PHS</scene> | + | |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>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FLP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= FLP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1flo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flo OCA], [http://www.ebi.ac.uk/pdbsum/1flo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1flo RCSB]</span> | ||
}} | }} | ||
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[[Category: Narendra, U.]] | [[Category: Narendra, U.]] | ||
[[Category: Rice, P A.]] | [[Category: Rice, P A.]] | ||
- | [[Category: PHS]] | ||
[[Category: domain-swapping]] | [[Category: domain-swapping]] | ||
[[Category: holliday-junction]] | [[Category: holliday-junction]] | ||
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[[Category: tyrosine recombinase]] | [[Category: tyrosine recombinase]] | ||
- | ''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 20:25:19 2008'' |
Revision as of 17:25, 30 March 2008
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, resolution 2.65Å | |||||||
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Sites: | , , , and | ||||||
Ligands: | , , , , | ||||||
Gene: | FLP1 (Saccharomyces cerevisiae) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
FLP RECOMBINASE-HOLLIDAY JUNCTION COMPLEX I
Overview
The crystal structure of a Flp recombinase tetramer bound to a Holliday junction intermediate has been determined at 2.65 A resolution. Only one of Flp's two domains, containing the active site, is structurally related to other lambda integrase family site-specific recombinases, such as Cre. The Flp active site differs, however, in that the helix containing the nucleophilic tyrosine is domain swapped, such that it cuts its DNA target in trans. The Flp tetramer displays pseudo four-fold symmetry matching that of the square planar Holliday junction substrate. This tetramer is stabilized by additional novel trans interactions among monomers. The structure illustrates how mechanistic unity is maintained on a chemical level while allowing for substantial variation on the structural level within a family of enzymes.
About this Structure
1FLO is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of a Flp recombinase-Holliday junction complex: assembly of an active oligomer by helix swapping., Chen Y, Narendra U, Iype LE, Cox MM, Rice PA, Mol Cell. 2000 Oct;6(4):885-97. PMID:11090626
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