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2f7t
From Proteopedia
(Difference between revisions)
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<StructureSection load='2f7t' size='340' side='right'caption='[[2f7t]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2f7t' size='340' side='right'caption='[[2f7t]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2f7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2f7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_mauritiana Drosophila mauritiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F7T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7t OCA], [https://pdbe.org/2f7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f7t RCSB], [https://www.ebi.ac.uk/pdbsum/2f7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f7t ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7t OCA], [https://pdbe.org/2f7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f7t RCSB], [https://www.ebi.ac.uk/pdbsum/2f7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f7t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MOS1T_DROMA MOS1T_DROMA] Mediates transposition of transposon Mos1 by a 'cut and paste' mechanism. Transposases are sequence-specific nucleases and strand transferases that catalyze transposition through an ordered series of events: sequence-specific binding of transposase to the terminal inverted repeats (IR) present at each end of the transposon, pairing of the transposon IRs in a paired-end complex (PEC), cleavage of one or both DNA strands at each transposon end, capture of target DNA, and strand transfer to insert the transposon at a new site. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f7t ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f7t ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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<ref>PMID:16511570</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2f7t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Transposase 3D structures|Transposase 3D structures]] | *[[Transposase 3D structures|Transposase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila mauritiana]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dawson | + | [[Category: Dawson A]] |
| - | [[Category: Finnegan | + | [[Category: Finnegan DJ]] |
| - | [[Category: Richardson | + | [[Category: Richardson JM]] |
| - | [[Category: Taylor | + | [[Category: Taylor P]] |
| - | [[Category: Walkinshaw | + | [[Category: Walkinshaw MD]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the catalytic domain of Mos1 mariner transposase
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