Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function.
Journal, issue, pages	Nature, Vol. 530, Issue 7590, Page 358-361, Year 2016
Publish date	Feb 18, 2016
Authors	Allison Ballandras-Colas / Monica Brown / Nicola J Cook / Tamaria G Dewdney / Borries Demeler / Peter Cherepanov / Dmitry Lyumkis / Alan N Engelman /
PubMed Abstract	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- ...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.
External links	Nature / PubMed:26887496 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.5 - 6.0 Å
Structure data	EMDB-6440: Three-dimensional structure of the full MMTV intasome Method: EM (single particle) / Resolution: 6.0 Å 6441 3jca EMDB-6441: Three-dimensional structure of the core MMTV intasome PDB-3jca: Core model of the Mouse Mammary Tumor Virus intasome Method: EM (single particle) / Resolution: 4.8 Å PDB-5cz1: Crystal structure of the catalytic core domain of MMTV integrase Method: X-RAY DIFFRACTION / Resolution: 1.7 Å PDB-5cz2: Crystal structure of a two-domain fragment of MMTV integrase Method: X-RAY DIFFRACTION / Resolution: 2.72 Å PDB-5d7u: Crystal structure of the C-terminal domain of MMTV integrase Method: X-RAY DIFFRACTION / Resolution: 1.5 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-HOH: WATER ChemComp-MG: Unknown entry ChemComp-IPA: ISOPROPYL ALCOHOL / alkaloid*YM
Source	mouse mammary tumor virus mouse mammary tumor virus (strain br6)
Keywords	VIRAL PROTEIN / integration / retrovirus / integrase / intasome / HYDROLASE / POL / catalytic core domain / amino terminal domain / zinc binding