3os2: Difference between revisions
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[[ | ==PFV target capture complex (TCC) at 3.32 A resolution== | ||
<StructureSection load='3os2' size='340' side='right' caption='[[3os2]], [[Resolution|resolution]] 3.32Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3os2]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OS2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3os0|3os0]], [[3os1|3os1]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11963 Human spumaretrovirus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3os2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3os2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3os2 RCSB], [http://www.ebi.ac.uk/pdbsum/3os2 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To establish productive infection, a retrovirus must insert a DNA replica of its genome into host cell chromosomal DNA. This process is operated by the intasome, a nucleoprotein complex composed of an integrase tetramer (IN) assembled on the viral DNA ends. The intasome engages chromosomal DNA within a target capture complex to carry out strand transfer, irreversibly joining the viral and cellular DNA molecules. Although several intasome/transpososome structures from the DDE(D) recombinase superfamily have been reported, the mechanics of target DNA capture and strand transfer by these enzymes remained unclear. Here we report crystal structures of the intasome from prototype foamy virus in complex with target DNA, elucidating the pre-integration target DNA capture and post-catalytic strand transfer intermediates of the retroviral integration process. The cleft between IN dimers within the intasome accommodates chromosomal DNA in a severely bent conformation, allowing widely spaced IN active sites to access the scissile phosphodiester bonds. Our results resolve the structural basis for retroviral DNA integration and provide a framework for the design of INs with altered target sequences. | |||
The mechanism of retroviral integration from X-ray structures of its key intermediates.,Maertens GN, Hare S, Cherepanov P Nature. 2010 Nov 11;468(7321):326-9. PMID:21068843<ref>PMID:21068843</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Retroviral Integrase|Retroviral Integrase]] | *[[Retroviral Integrase|Retroviral Integrase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Human spumaretrovirus]] | [[Category: Human spumaretrovirus]] | ||
[[Category: Cherepanov, P | [[Category: Cherepanov, P]] | ||
[[Category: Hare, S | [[Category: Hare, S]] | ||
[[Category: Maertens, G N | [[Category: Maertens, G N]] | ||
[[Category: Dna integration]] | [[Category: Dna integration]] | ||
[[Category: Dna-binding]] | [[Category: Dna-binding]] | ||
Revision as of 13:53, 9 December 2014
PFV target capture complex (TCC) at 3.32 A resolutionPFV target capture complex (TCC) at 3.32 A resolution
Structural highlights
Publication Abstract from PubMedTo establish productive infection, a retrovirus must insert a DNA replica of its genome into host cell chromosomal DNA. This process is operated by the intasome, a nucleoprotein complex composed of an integrase tetramer (IN) assembled on the viral DNA ends. The intasome engages chromosomal DNA within a target capture complex to carry out strand transfer, irreversibly joining the viral and cellular DNA molecules. Although several intasome/transpososome structures from the DDE(D) recombinase superfamily have been reported, the mechanics of target DNA capture and strand transfer by these enzymes remained unclear. Here we report crystal structures of the intasome from prototype foamy virus in complex with target DNA, elucidating the pre-integration target DNA capture and post-catalytic strand transfer intermediates of the retroviral integration process. The cleft between IN dimers within the intasome accommodates chromosomal DNA in a severely bent conformation, allowing widely spaced IN active sites to access the scissile phosphodiester bonds. Our results resolve the structural basis for retroviral DNA integration and provide a framework for the design of INs with altered target sequences. The mechanism of retroviral integration from X-ray structures of its key intermediates.,Maertens GN, Hare S, Cherepanov P Nature. 2010 Nov 11;468(7321):326-9. PMID:21068843[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human spumaretrovirus
- Cherepanov, P
- Hare, S
- Maertens, G N
- Dna integration
- Dna-binding
- Endonuclease
- Hhcc motif
- Metal-binding
- Multifunctional enzyme
- Nuclease
- Nucleotidyltransferase
- Nucleus
- Protein-dna complex
- Recombination
- Recombination-dna complex
- Tetramer
- Transferase
- Viral nucleoprotein
- Viral protein
- Virion
- Zinc binding