2f7t
From Proteopedia
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|PDB= 2f7t |SIZE=350|CAPTION= <scene name='initialview01'>2f7t</scene>, resolution 2.25Å | |PDB= 2f7t |SIZE=350|CAPTION= <scene name='initialview01'>2f7t</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7t OCA], [http://www.ebi.ac.uk/pdbsum/2f7t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f7t RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Taylor, P.]] | [[Category: Taylor, P.]] | ||
[[Category: Walkinshaw, M D.]] | [[Category: Walkinshaw, M D.]] | ||
| - | [[Category: MG]] | ||
[[Category: ddd motif]] | [[Category: ddd motif]] | ||
[[Category: rnase-h like fold]] | [[Category: rnase-h like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:59:03 2008'' |
Revision as of 23:59, 30 March 2008
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| , resolution 2.25Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the catalytic domain of Mos1 mariner transposase
Overview
We present the crystal structure of the catalytic domain of Mos1 transposase, a member of the Tc1/mariner family of transposases. The structure comprises an RNase H-like core, bringing together an aspartic acid triad to form the active site, capped by N- and C-terminal alpha-helices. We have solved structures with either one Mg2+ or two Mn2+ ions in the active site, consistent with a two-metal mechanism for catalysis. The lack of hairpin-stabilizing structural motifs is consistent with the absence of a hairpin intermediate in Mos1 excision. We have built a model for the DNA-binding domain of Mos1 transposase, based on the structure of the bipartite DNA-binding domain of Tc3 transposase. Combining this with the crystal structure of the catalytic domain provides a model for the paired-end complex formed between a dimer of Mos1 transposase and inverted repeat DNA. The implications for the mechanisms of first and second strand cleavage are discussed.
About this Structure
2F7T is a Single protein structure of sequence from Drosophila mauritiana. Full crystallographic information is available from OCA.
Reference
Mechanism of Mos1 transposition: insights from structural analysis., Richardson JM, Dawson A, O'Hagan N, Taylor P, Finnegan DJ, Walkinshaw MD, EMBO J. 2006 Mar 22;25(6):1324-34. Epub 2006 Mar 2. PMID:16511570
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