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An S-layer (surface layer) is a cell surface protein layer found in many different bacteria and in some archaea, where it serves as the cell wall. All S-layers are made up of a two-dimensional array of proteins and have a crystalline appearance, the symmetry of which differs between species.
Bacteria have microcompartments, quasi-organelles enclosed in protein shells such as encapsulin protein cages, [4] [5] while both bacteria and some archaea have gas vesicles. [6] Prokaryotes have simple cell skeletons. These are highly diverse, and contain homologues of the eukaryote proteins actin and tubulin. The cytoskeleton provides the ...
An S-layer (surface layer) is a part of the cell envelope found in almost all archaea, as well as in many types of bacteria. [1] [2] The S-layers of both archaea and bacteria consists of a monomolecular layer composed of only one (or, in a few cases, two) identical proteins or glycoproteins. [3]
Others span cell membranes and are commonly found in porins. Porin-like barrel structures are encoded by as many as 2–3% of the genes in Gram-negative bacteria. [ 1 ] It has been shown that more than 600 proteins with various function such as oxidase, dismutase, and amylase contain the beta barrel structure.
Porins are water-filled pores and channels found in the membranes of bacteria and eukaryotes. Porin-like channels have also been discovered in archaea. [7] Note that the term "nucleoporin" refers to unrelated proteins that facilitate transport through nuclear pores in the nuclear envelope.
Proteins are shown in blue and the single RNA strand in orange. [1] The prokaryotic small ribosomal subunit, or 30S subunit, is the smaller subunit of the 70S ribosome found in prokaryotes. It is a complex of the 16S ribosomal RNA (rRNA) and 19 proteins. [1] This complex is implicated in the binding of transfer RNA to messenger RNA (mRNA). [2]
Flagellin-like structural proteins are found in other portions of the flagellum, such as the hook (flgE; ), the rod at the base, and the cap at the top. [ 7 ] The middle part of E. coli (and related) flagellin, D3, displays a beta-folium fold and appears to maintain flagellar stability.
The enzyme cytochrome c oxidase or Complex IV (was EC 1.9.3.1, now reclassified as a translocase EC 7.1.1.9) is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes.