5JYG
Cryo-EM structure of the MamK filament at 6.5 A
Summary for 5JYG
Entry DOI | 10.2210/pdb5jyg/pdb |
EMDB information | 8180 |
Descriptor | Actin-like ATPase, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | actin-like, magnetosome, bacteria, structural protein |
Biological source | Magnetospirillum magneticum (strain AMB-1 / ATCC 700264) |
Total number of polymer chains | 14 |
Total formula weight | 533507.60 |
Authors | Bergeron, J.R.C.,Hutto, R.,Kollman, J.M. (deposition date: 2016-05-13, release date: 2016-07-27, Last modification date: 2024-03-06) |
Primary citation | Bergeron, J.R.,Hutto, R.,Ozyamak, E.,Hom, N.,Hansen, J.,Draper, O.,Byrne, M.E.,Keyhani, S.,Komeili, A.,Kollman, J.M. Structure of the magnetosome-associated actin-like MamK filament at subnanometer resolution. Protein Sci., 26:93-102, 2017 Cited by PubMed Abstract: Magnetotactic bacteria possess cellular compartments called magnetosomes that sense magnetic fields. Alignment of magnetosomes in the bacterial cell is necessary for their function, and this is achieved through anchoring of magnetosomes to filaments composed of the protein MamK. MamK is an actin homolog that polymerizes upon ATP binding. Here, we report the structure of the MamK filament at ∼6.5 Å, obtained by cryo-Electron Microscopy. This structure confirms our previously reported double-stranded, nonstaggered architecture, and reveals the molecular basis for filament formation. While MamK is closest in sequence to the bacterial actin MreB, the longitudinal contacts along each MamK strand most closely resemble those of eukaryotic actin. In contrast, the cross-strand interface, with a surprisingly limited set of contacts, is novel among actin homologs and gives rise to the nonstaggered architecture. PubMed: 27391173DOI: 10.1002/pro.2979 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (6.5 Å) |
Structure validation
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