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| | <StructureSection load='5cz2' size='340' side='right'caption='[[5cz2]], [[Resolution|resolution]] 2.72Å' scene=''> | | <StructureSection load='5cz2' size='340' side='right'caption='[[5cz2]], [[Resolution|resolution]] 2.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cz2]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Mmtv Mmtv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CZ2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cz2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mouse_mammary_tumor_virus_(STRAIN_BR6) Mouse mammary tumor virus (STRAIN BR6)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CZ2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.72Å</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=11758 MMTV])</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5cz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cz2 OCA], [http://pdbe.org/5cz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cz2 RCSB], [http://www.ebi.ac.uk/pdbsum/5cz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cz2 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=5cz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cz2 OCA], [https://pdbe.org/5cz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cz2 RCSB], [https://www.ebi.ac.uk/pdbsum/5cz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cz2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/POL_MMTVB POL_MMTVB]] During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. | + | [https://www.uniprot.org/uniprot/POL_MMTVB POL_MMTVB] During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mmtv]]
| + | [[Category: Ballandras-Colas A]] |
| - | [[Category: Ballandras-Colas, A]] | + | [[Category: Cherepanov P]] |
| - | [[Category: Cherepanov, P]] | + | [[Category: Cook N]] |
| - | [[Category: Cook, N]] | + | [[Category: Engelman A]] |
| - | [[Category: Engelman, A]] | + | |
| - | [[Category: Amino terminal domain]]
| + | |
| - | [[Category: Catalytic core domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Integrase]]
| + | |
| - | [[Category: Pol]]
| + | |
| - | [[Category: Retrovirus]]
| + | |
| - | [[Category: Zinc binding]]
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| Structural highlights
Function
POL_MMTVB During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.
Publication Abstract from PubMed
Retroviral integrase catalyses the integration of viral DNA into host target DNA, which is an essential step in the life cycle of all retroviruses. Previous structural characterization of integrase-viral DNA complexes, or intasomes, from the spumavirus prototype foamy virus revealed a functional integrase tetramer, and it is generally believed that intasomes derived from other retroviral genera use tetrameric integrase. However, the intasomes of orthoretroviruses, which include all known pathogenic species, have not been characterized structurally. Here, using single-particle cryo-electron microscopy and X-ray crystallography, we determine an unexpected octameric integrase architecture for the intasome of the betaretrovirus mouse mammary tumour virus. The structure is composed of two core integrase dimers, which interact with the viral DNA ends and structurally mimic the integrase tetramer of prototype foamy virus, and two flanking integrase dimers that engage the core structure via their integrase carboxy-terminal domains. Contrary to the belief that tetrameric integrase components are sufficient to catalyse integration, the flanking integrase dimers were necessary for mouse mammary tumour virus integrase activity. The integrase octamer solves a conundrum for betaretroviruses as well as alpharetroviruses by providing critical carboxy-terminal domains to the intasome core that cannot be provided in cis because of evolutionarily restrictive catalytic core domain-carboxy-terminal domain linker regions. The octameric architecture of the intasome of mouse mammary tumour virus provides new insight into the structural basis of retroviral DNA integration.
Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function.,Ballandras-Colas A, Brown M, Cook NJ, Dewdney TG, Demeler B, Cherepanov P, Lyumkis D, Engelman AN Nature. 2016 Feb 18;530(7590):358-61. doi: 10.1038/nature16955. PMID:26887496[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ballandras-Colas A, Brown M, Cook NJ, Dewdney TG, Demeler B, Cherepanov P, Lyumkis D, Engelman AN. Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function. Nature. 2016 Feb 18;530(7590):358-61. doi: 10.1038/nature16955. PMID:26887496 doi:http://dx.doi.org/10.1038/nature16955
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