2rsl
From Proteopedia
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| - | [[Image:2rsl.jpg|left|200px]] | + | [[Image:2rsl.jpg|left|200px]] |
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| - | '''REFINEMENT OF GAMMA DELTA RESOLVASE REVEALS A STRIKINGLY FLEXIBLE MOLECULE''' | + | {{Structure |
| + | |PDB= 2rsl |SIZE=350|CAPTION= <scene name='initialview01'>2rsl</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''REFINEMENT OF GAMMA DELTA RESOLVASE REVEALS A STRIKINGLY FLEXIBLE MOLECULE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2RSL is a [ | + | 2RSL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1RSL. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSL OCA]. |
==Reference== | ==Reference== | ||
| - | Refinement of gamma delta resolvase reveals a strikingly flexible molecule., Rice PA, Steitz TA, Structure. 1994 May 15;2(5):371-84. PMID:[http:// | + | Refinement of gamma delta resolvase reveals a strikingly flexible molecule., Rice PA, Steitz TA, Structure. 1994 May 15;2(5):371-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8081753 8081753] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: site-specific recombinase]] | [[Category: site-specific 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 18:37:55 2008'' |
Revision as of 16:37, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
REFINEMENT OF GAMMA DELTA RESOLVASE REVEALS A STRIKINGLY FLEXIBLE MOLECULE
Overview
BACKGROUND: gamma delta resolvase is a 20.5 kDa enzyme that catalyzes a site-specific recombination in the second step of the transposition of the gamma delta transposon and requires no cofactors other than Mg2+ for activity. Dimers of resolvase bind cooperatively to DNA at three inverted repeat sequences of differing geometry but catalyze recombination at only one site. RESULTS: The structure of the catalytic domain of gamma delta resolvase, which provides the protein-protein interactions in the synaptic complex, has been refined to an R-factor of 20% at 2.3 A resolution. The structures of the three independent monomers in the asymmetric unit are similar but not identical. Differences occur in the positions of surface loops and in the overall twist of the central beta-sheet of the molecule. The crystal also gives two independent structures for the dimeric form of the molecule, which also show significant differences in the relative orientations of their subunits. CONCLUSION: Resolvase is an unusually flexible protein. This conformational adaptability may be necessary to allow each of the 12 resolvase subunits in the synaptic complex to play a different but specific role in wrapping DNA, binding sites of differing geometry and catalyzing recombination.
About this Structure
2RSL is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1RSL. Full crystallographic information is available from OCA.
Reference
Refinement of gamma delta resolvase reveals a strikingly flexible molecule., Rice PA, Steitz TA, Structure. 1994 May 15;2(5):371-84. PMID:8081753
Page seeded by OCA on Thu Mar 20 18:37:55 2008
