5YA6
Crystal structure of archaeal flagellin FlaB1 from Methanocaldococcus jannaschii
Summary for 5YA6
| Entry DOI | 10.2210/pdb5ya6/pdb |
| Related | 5Z1L |
| EMDB information | 6876 |
| Descriptor | Flagellin B1, CALCIUM ION (3 entities in total) |
| Functional Keywords | archaea, flagellum, flagellin, structural protein |
| Biological source | Methanocaldococcus jannaschii DSM 2661 |
| Total number of polymer chains | 2 |
| Total formula weight | 36971.23 |
| Authors | Meshcheryakov, V.A.,Wolf, M. (deposition date: 2017-08-30, release date: 2019-02-06, Last modification date: 2024-03-27) |
| Primary citation | Meshcheryakov, V.A.,Shibata, S.,Schreiber, M.T.,Villar-Briones, A.,Jarrell, K.F.,Aizawa, S.I.,Wolf, M. High-resolution archaellum structure reveals a conserved metal-binding site. Embo Rep., 20:-, 2019 Cited by PubMed Abstract: Many archaea swim by means of archaella. While the archaellum is similar in function to its bacterial counterpart, its structure, composition, and evolution are fundamentally different. Archaella are related to archaeal and bacterial type IV pili. Despite recent advances, our understanding of molecular processes governing archaellum assembly and stability is still incomplete. Here, we determine the structures of archaella by X-ray crystallography and cryo-EM The crystal structure of FlaB1 is the first and only crystal structure of any archaellin to date at a resolution of 1.5 Å, which is put into biological context by a cryo-EM reconstruction from archaella at 4 Å resolution created with helical single-particle analysis. Our results indicate that the archaellum is predominantly composed of FlaB1. We identify N-linked glycosylation by cryo-EM and mass spectrometry. The crystal structure reveals a highly conserved metal-binding site, which is validated by mass spectrometry and electron energy-loss spectroscopy. We show that the metal-binding site, which appears to be a widespread property of archaellin, is required for filament integrity. PubMed: 30898768DOI: 10.15252/embr.201846340 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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