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 the Borrelia Bacteriophage φBB1 Procapsid.
Journal, issue, pages	J Mol Biol, Vol. 435, Issue 24, Page 168323, Year 2023
Publish date	Dec 15, 2023
Authors	Jānis Rūmnieks / Tibor Füzik / Kaspars Tārs /
PubMed Abstract	Bacteriophages of Borrelia burgdorferi are a biologically important but under-investigated feature of the Lyme disease-causing spirochete. No virulent borrelial viruses have been identified, but all ...Bacteriophages of Borrelia burgdorferi are a biologically important but under-investigated feature of the Lyme disease-causing spirochete. No virulent borrelial viruses have been identified, but all B. burgdorferi isolates carry a prophage φBB1 as resident circular plasmids. Like its host, the φBB1 phage is quite distinctive and shares little sequence similarity with other known bacteriophages. We expressed φBB1 head morphogenesis proteins in Escherichia coli which resulted in assembly of homogeneous prolate procapsid structures and used cryo-electron microscopy to determine the three-dimensional structure of these particles. The φBB1 procapsids consist of 415 copies of the major capsid protein and an equal combined number of three homologous capsid decoration proteins that form trimeric knobs on the outside of the particle. One of the end vertices of the particle is occupied by a portal assembled from twelve copies of the portal protein. The φBB1 scaffolding protein is entirely α-helical and has an elongated shape with a small globular domain in the middle. Within the tubular section of the procapsid, the internal scaffold is built of stacked rings, each composed of 32 scaffolding protein molecules, which run in opposite directions from both caps with a heterogeneous part in the middle. Inside the portal-containing cap, the scaffold is organized asymmetrically with ten scaffolding protein molecules bound to the portal. The φBB1 procapsid structure provides better insight into the vast structural diversity of bacteriophages and presents clues of how elongated bacteriophage particles might be assembled.
External links	J Mol Biol / PubMed:37866476
Methods	EM (single particle)
Resolution	2.34 - 10.62 Å
Structure data	17669 8pho EMDB-17669, PDB-8pho: Portal from the Borrelia bacteriophage BB1 procapsid Method: EM (single particle) / Resolution: 2.34 Å 17670 8php EMDB-17670, PDB-8php: Portal from the Borrelia bacteriophage BB1 procapsid with bound scaffold protein Method: EM (single particle) / Resolution: 2.56 Å 17671 8phq EMDB-17671, PDB-8phq: Top cap of the Borrelia bacteriophage BB1 procapsid, fivefold-symmetrized outer shell Method: EM (single particle) / Resolution: 2.69 Å 17672 8phr EMDB-17672, PDB-8phr: Middle part of the Borrelia bacteriophage BB1 procapsid, tenfold-symmetrized outer shell Method: EM (single particle) / Resolution: 2.65 Å 17673 8phs EMDB-17673, PDB-8phs: Bottom cap of the Borrelia bacteriophage BB1 procapsid, fivefold-symmetrized outer shell Method: EM (single particle) / Resolution: 2.82 Å 17674 8pht EMDB-17674, PDB-8pht: Scaffold rings inside the Borrelia bacteriophage BB1 procapsid Method: EM (single particle) / Resolution: 6.37 Å 17675 8phu EMDB-17675, PDB-8phu: Asymmetric structure of the portal-containing cap of the Borrelia bacteriophage BB1 procapsid Method: EM (single particle) / Resolution: 7.41 Å 17739 8pkh EMDB-17739, PDB-8pkh: Borrelia bacteriophage BB1 procapsid, fivefold-symmetrized outer shell Method: EM (single particle) / Resolution: 3.35 Å 18518 8qo0 EMDB-18518, PDB-8qo0: Asymmetric structure of the Borrelia bacteriophage BB1 procapsid, 3D class 2 Method: EM (single particle) / Resolution: 10.62 Å 18519 8qo1 EMDB-18519, PDB-8qo1: Asymmetric structure of the Borrelia bacteriophage BB1 procapsid, 3D class 3 Method: EM (single particle) / Resolution: 9.76 Å
Chemicals	ChemComp-HOH: WATER
Source	borreliella burgdorferi b31 (bacteria)
Keywords	VIRAL PROTEIN / Bacteriophage / portal / DNA packaging / scaffold / capsid / procapsid