| Literature DB >> 27391173 |
Julien R C Bergeron1, Rachel Hutto1, Ertan Ozyamak2, Nancy Hom3, Jesse Hansen4, Olga Draper2, Meghan E Byrne2, Sepehr Keyhani2, Arash Komeili2, Justin M Kollman1.
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.Entities:
Keywords: Cryo-EM; actin; filaments; magnetosome
Mesh:
Substances:
Year: 2016 PMID: 27391173 PMCID: PMC5192964 DOI: 10.1002/pro.2979
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725