hide
Free keywords:
Electron crystallography; Electron microscopy; Electron tomography; Surface layer proteins from bacteria and archaea; S-layer cell wall interactions; S-layer homology domain; S-layer structure; Slh domain; Stability of s-layer proteins; High resolution structure of s-layers.; Eubacterium thermotoga-maritima; Thermus-thermophilus hb8; Nucleotide-sequence analysis; Bacillus-brevis 47; 3-dimensional structure; S-layer; Escherichia-coli; Deinococcus-radiodurans; Outer-membrane; Corynebacterium-glutamicum.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
Abstract:
Surface layers (S-layers) from Bacteria and Archaea are built from protein molecules arrayed in a two-dimensional lattice, forming the outermost cell wall layer in many prokaryotes. In almost half a century of S-layer research a wealth of structural, biochemical, and genetic data have accumulated, but it has not been possible to correlate sequence data with the tertiary structure of S-layer proteins to date. In this paper, some highlights of structural aspects of archaeal and bacterial S-layers that allow us to draw some conclusions on molecular properties are reviewed. We focus on the structural requirements for the extraordinary stability of many S-layer proteins, the structural and functional aspects of the S-layer homology domain found in S-layers, extracellular enzymes and related functional proteins, and outer membrane proteins, and the molecular interactions of S-layer proteins with other cell wall components. Finally, the perspectives and requirements for structural research on S-layers, which indicate that the investigation of isolated protein domains will be a prerequisite for solving S-layer structures at atomic resolution, are discussed. (C) 1998 Academic Press. [References: 181]
