3hot

From Proteopedia

(Difference between revisions)

Revision as of 15:52, 1 November 2023

Crystal structure of the Mos1 mariner paired end complex with Mn

Structural highlights

3hot is a 8 chain structure with sequence from Drosophila mauritiana and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.25Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A key step in cut-and-paste DNA transposition is the pairing of transposon ends before the element is excised and inserted at a new site in its host genome. Crystallographic analyses of the paired-end complex (PEC) formed from precleaved transposon ends and the transposase of the eukaryotic element Mos1 reveals two parallel ends bound to a dimeric enzyme. The complex has a trans arrangement, with each transposon end recognized by the DNA binding region of one transposase monomer and by the active site of the other monomer. Two additional DNA duplexes in the crystal indicate likely binding sites for flanking DNA. Biochemical data provide support for a model of the target capture complex and identify Arg186 to be critical for target binding. Mixing experiments indicate that a transposase dimer initiates first-strand cleavage and suggest a pathway for PEC formation.

Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote.,Richardson JM, Colloms SD, Finnegan DJ, Walkinshaw MD Cell. 2009 Sep 18;138(6):1096-108. PMID:19766564^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Richardson JM, Colloms SD, Finnegan DJ, Walkinshaw MD. Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote. Cell. 2009 Sep 18;138(6):1096-108. PMID:19766564 doi:10.1016/j.cell.2009.07.012

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hot"

Categories: Drosophila mauritiana | Large Structures | Synthetic construct | Richardson JM | Walkinshaw MD

@@ Line 3: / Line 3: @@
 <StructureSection load='3hot' size='340' side='right'caption='[[3hot]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3hot]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Droma Droma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HOT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3hot]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_mauritiana Drosophila mauritiana] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HOT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.25&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5IU:5-IODO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>5IU</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5IU:5-IODO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>5IU</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hos|3hos]]</div></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=3hot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hot OCA], [https://pdbe.org/3hot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hot RCSB], [https://www.ebi.ac.uk/pdbsum/3hot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hot ProSAT]</span></td></tr>
 </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.
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Droma]]
+[[Category: Drosophila mauritiana]]
 [[Category: Large Structures]]
-[[Category: Richardson, J M]]
+[[Category: Synthetic construct]]
-[[Category: Walkinshaw, M D]]
+[[Category: Richardson JM]]
-[[Category: Dna binding protein-dna complex]]
+[[Category: Walkinshaw MD]]
-[[Category: Inverted repeat dna]]
-[[Category: Protein-dna complex]]
-[[Category: Synaptic complex]]
-[[Category: Transferase]]
-[[Category: Transposase]]

3hot

From Proteopedia

Revision as of 15:52, 1 November 2023

Crystal structure of the Mos1 mariner paired end complex with Mn

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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