7PTP

In-situ structure of pentameric S-layer protein

Summary for 7PTP

• Entry DOI: 10.2210/pdb7ptp/pdb
• EMDB information: 13632
• Descriptor: Cell surface glycoprotein (1 entity in total)
• Functional Keywords: s-layer csg, structural protein
• Biological source: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
• Total number of polymer chains: 5
• Total formula weight: 408778.01

Authors

von Kuegelgen, A.,Bharat, T.A.M. (deposition date: 2021-09-27, release date: 2021-12-15, Last modification date: 2024-07-17)

Primary citation

von Kugelgen, A.,Alva, V.,Bharat, T.A.M.
Complete atomic structure of a native archaeal cell surface.
Cell Rep, 37:110052-110052, 2021

PubMed Abstract: Many prokaryotic cells are covered by an ordered, proteinaceous, sheet-like structure called a surface layer (S-layer). S-layer proteins (SLPs) are usually the highest copy number macromolecules in prokaryotes, playing critical roles in cellular physiology such as blocking predators, scaffolding membranes, and facilitating environmental interactions. Using electron cryomicroscopy of two-dimensional sheets, we report the atomic structure of the S-layer from the archaeal model organism Haloferax volcanii. This S-layer consists of a hexagonal array of tightly interacting immunoglobulin-like domains, which are also found in SLPs across several classes of archaea. Cellular tomography reveal that the S-layer is nearly continuous on the cell surface, completed by pentameric defects in the hexagonal lattice. We further report the atomic structure of the SLP pentamer, which shows markedly different relative arrangements of SLP domains needed to complete the S-layer. Our structural data provide a framework for understanding cell surfaces of archaea at the atomic level.

PubMed: 34818541
DOI: 10.1016/j.celrep.2021.110052

Experimental method

ELECTRON MICROSCOPY (11.58 Å)