1flo
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of a Flp recombinase tetramer bound to a Holliday | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, Y.]] | [[Category: Chen, Y.]] | ||
| - | [[Category: Cox, M | + | [[Category: Cox, M M.]] |
| - | [[Category: Iype, L | + | [[Category: Iype, L E.]] |
[[Category: Narendra, U.]] | [[Category: Narendra, U.]] | ||
| - | [[Category: Rice, P | + | [[Category: Rice, P A.]] |
[[Category: PHS]] | [[Category: PHS]] | ||
[[Category: domain-swapping]] | [[Category: domain-swapping]] | ||
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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 Thu Feb 21 12:39:57 2008'' |
Revision as of 10:39, 21 February 2008
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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 with as ligand. Known structural/functional Sites: , , , and . 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
Page seeded by OCA on Thu Feb 21 12:39:57 2008
