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	Structure of AcMNPV nucleocapsid reveals DNA portal organization and packaging apparatus of circular dsDNA baculovirus.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 4844, Year 2025
Publish date	May 24, 2025
Authors	Gregory Effantin / Eaazhisai Kandiah / Martin Pelosse /
PubMed Abstract	Baculoviruses are large DNA viruses found in nature propagating amongst insects and lepidoptera in particular. They have been studied for decades and are nowadays considered as invaluable ...Baculoviruses are large DNA viruses found in nature propagating amongst insects and lepidoptera in particular. They have been studied for decades and are nowadays considered as invaluable biotechnology tools used as biopesticides, recombinant expression systems or delivery vehicle for gene therapy. However, little is known about the baculovirus nucleocapsid assembly at a molecular level. Here, we solve the whole structure of the Autographa californica multiple nucleopolyhedrovirus (AcMNPV) nucleocapsid by applying cryo-electron microscopy (CryoEM) combined with de novo modelling and Alphafold predictions. Our structure completes prior observations and elucidates the intricate architecture of the apical cap, unravelling the organization of a DNA portal featuring intriguing symmetry mismatches between its core and vertex. The core, closing the capsid at the apex, holds two DNA helices of the viral genome tethered to Ac54 proteins. Different symmetry components at the apical cap and basal structure are constituted of the same building block, made of Ac101/Ac144, proving the versatility of this modular pair. The crown forming the portal vertex displays a C21 symmetry and contains, amongst others, the motor-like protein Ac66. Our findings support the viral portal to be involved in DNA packaging, probably in conjunction with other parts of a larger DNA packaging apparatus.
External links	Nat Commun / PubMed:40413174 / PubMed Central
Methods	EM (helical sym.) / EM (single particle)
Resolution	3.0 - 6.6 Å
Structure data	51771 9h1s EMDB-51771, PDB-9h1s: AcMNPV helical nucleocapsid Method: EM (helical sym.) / Resolution: 3.0 Å 51791 9h2a EMDB-51791, PDB-9h2a: AcMNPV complete basal cap Method: EM (single particle) / Resolution: 5.2 Å 51792 9h2b EMDB-51792, PDB-9h2b: AcMNPV basal cap - C14 anchor complex only Method: EM (single particle) / Resolution: 4.1 Å 51793 9h2c EMDB-51793, PDB-9h2c: AcMNPV basal cap - C7 plug only Method: EM (single particle) / Resolution: 3.4 Å EMDB-51794: AcMNPV apical cap - C2 core only Method: EM (single particle) / Resolution: 6.0 Å 51803 9h2h EMDB-51803, PDB-9h2h: AcMNPV apical cap - composite map of the C2 plug Method: EM (single particle) / Resolution: 6.1 Å EMDB-51805: AcMNPV apical cap - C2 plug only -consensus 3D map Method: EM (single particle) / Resolution: 6.6 Å EMDB-51806: AcMNPV apical cap - C2 plug only - focused map 1 Method: EM (single particle) / Resolution: 6.1 Å EMDB-51807: AcMNPV apical cap - C2 plug focused map 2 Method: EM (single particle) / Resolution: 6.5 Å 51808 9h2j EMDB-51808, PDB-9h2j: AcMNPV apical cap - C14 anchor complex only Method: EM (single particle) / Resolution: 4.7 Å 51809 9h2k EMDB-51809, PDB-9h2k: AcMNPV apical cap - C21 ring Method: EM (single particle) / Resolution: 3.5 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	autographa californica nucleopolyhedrovirus
Keywords	VIRUS / nucleocapsid / helical