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	The evolution of archaeal flagellar filaments.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 120, Issue 28, Page e2304256120, Year 2023
Publish date	Jul 11, 2023
Authors	Mark A B Kreutzberger / Virginija Cvirkaite-Krupovic / Ying Liu / Diana P Baquero / Junfeng Liu / Ravi R Sonani / Chris R Calladine / Fengbin Wang / Mart Krupovic / Edward H Egelman /
PubMed Abstract	Flagellar motility has independently arisen three times during evolution: in bacteria, archaea, and eukaryotes. In prokaryotes, the supercoiled flagellar filaments are composed largely of a single ...Flagellar motility has independently arisen three times during evolution: in bacteria, archaea, and eukaryotes. In prokaryotes, the supercoiled flagellar filaments are composed largely of a single protein, bacterial or archaeal flagellin, although these two proteins are not homologous, while in eukaryotes, the flagellum contains hundreds of proteins. Archaeal flagellin and archaeal type IV pilin are homologous, but how archaeal flagellar filaments (AFFs) and archaeal type IV pili (AT4Ps) diverged is not understood, in part, due to the paucity of structures for AFFs and AT4Ps. Despite having similar structures, AFFs supercoil, while AT4Ps do not, and supercoiling is essential for the function of AFFs. We used cryo-electron microscopy to determine the atomic structure of two additional AT4Ps and reanalyzed previous structures. We find that all AFFs have a prominent 10-strand packing, while AT4Ps show a striking structural diversity in their subunit packing. A clear distinction between all AFF and all AT4P structures involves the extension of the N-terminal α-helix with polar residues in the AFFs. Additionally, we characterize a flagellar-like AT4P from with filament and subunit structure similar to that of AFFs which can be viewed as an evolutionary link, showing how the structural diversity of AT4Ps likely allowed for an AT4P to evolve into a supercoiling AFF.
External links	Proc Natl Acad Sci U S A / PubMed:37399404 / PubMed Central
Methods	EM (helical sym.) / EM (single particle)
Resolution	2.9 - 4.3 Å
Structure data	26158 7txi EMDB-26158, PDB-7txi: Cryo-EM of A. pernix flagellum Method: EM (helical sym.) / Resolution: 3.5 Å 29215 8fj5 EMDB-29215, PDB-8fj5: Structure of the Haloferax volcanii archaeal type IV pilus Method: EM (helical sym.) / Resolution: 2.9 Å 29246 8fjs EMDB-29246, PDB-8fjs: Structure of the Saccharolobus solfataricus archaeal type IV pilus at 3 Angstrom resolution Method: EM (helical sym.) / Resolution: 3.0 Å 29247 8fk0 EMDB-29247, PDB-8fk0: Asymmetric cryo-EM structure of a curved Saccharolobus solfataricus type IV pilus Method: EM (single particle) / Resolution: 4.0 Å 29249 8fk7 EMDB-29249, PDB-8fk7: Structure of the Pyrobaculum calidifontis flagellar-like archaeal type IV pilus Method: EM (helical sym.) / Resolution: 4.3 Å 40060 8gi2 EMDB-40060, PDB-8gi2: Cryo-EM structure of Natrinema sp. J7-2 Type IV pilus Method: EM (helical sym.) / Resolution: 3.0 Å
Source	aeropyrum pernix (archaea) Haloferax volcanii (archaea) haloferax volcanii (strain atcc 29605 / dsm 3757 / jcm 8879 / nbrc 14742 / ncimb 2012 / vkm b-1768 / ds2) (archaea) saccharolobus solfataricus (archaea) pyrobaculum calidifontis (archaea) natrinema sp. j7-2 (archaea)
Keywords	STRUCTURAL PROTEIN / helical symmetry / flagellum / cell appendage / Archaea / type IV pili / MOTOR PROTEIN / Helical / Pili / Natrinema / PROTEIN FIBRIL