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	High-resolution structures of HIV-1 Gag cleavage mutants determine structural switch for virus maturation.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 115, Issue 40, Page E9401-E9410, Year 2018
Publish date	Oct 2, 2018
Authors	Simone Mattei / Aaron Tan / Bärbel Glass / Barbara Müller / Hans-Georg Kräusslich / John A G Briggs /
PubMed Abstract	HIV-1 maturation occurs via multiple proteolytic cleavages of the Gag polyprotein, causing rearrangement of the virus particle required for infectivity. Cleavage results in beta-hairpin formation at ...HIV-1 maturation occurs via multiple proteolytic cleavages of the Gag polyprotein, causing rearrangement of the virus particle required for infectivity. Cleavage results in beta-hairpin formation at the N terminus of the CA (capsid) protein and loss of a six-helix bundle formed by the C terminus of CA and the neighboring SP1 peptide. How individual cleavages contribute to changes in protein structure and interactions, and how the mature, conical capsid forms, are poorly understood. Here, we employed cryoelectron tomography to determine morphology and high-resolution CA lattice structures for HIV-1 derivatives in which Gag cleavage sites are mutated. These analyses prompt us to revise current models for the crucial maturation switch. Unlike previously proposed, cleavage on either terminus of CA was sufficient, in principle, for lattice maturation, while complete processing was needed for conical capsid formation. We conclude that destabilization of the six-helix bundle, rather than beta-hairpin formation, represents the main determinant of structural maturation.
External links	Proc Natl Acad Sci U S A / PubMed:30217893 / PubMed Central
Methods	EM (subtomogram averaging) / EM (tomography)
Resolution	3.7 - 24.0 Å
Structure data	EMDB-0164: Immature CA domain from HIV-1 MA-SP1 Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 4.0 Å EMDB-0165: Immature CA domain from HIV-1 MA-CA Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 3.7 Å EMDB-0166: Immature CA domain from HIV-1 CA-NC Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 4.5 Å EMDB-0167: Mature CA domain hexamer from HIV-1 MA-CA Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 8.3 Å EMDB-0168: Mature CA domain hexamer from HIV-1 CA-NC Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 9.7 Å EMDB-0169: Mature CA domain hexamer from HIV-1 CA-SP1 Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 7.9 Å EMDB-0170: Mature CA domain pentamer from HIV-1 CA-NC Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 22.0 Å EMDB-0171: Mature CA domain pentamer from HIV-1 CA-SP1 Gag proteolytic cleavage mutant virus particles Method: EM (subtomogram averaging) / Resolution: 24.0 Å EMDB-13079: Representative cryo-electron tomogram of HIV-1 MA-SP1 particles Method: EM (tomography) EMDB-13080: Representative cryo-electron tomogram of HIV-1 MA-CA particles Method: EM (tomography)
Source	Homo sapiens (human)