Protein Family Models

The Linocin_M18 is found in eubacteria and archaea [1,2]. These proteins, referred to as encapsulins, form nanocompartments within the bacterium which contain ferritin-like proteins or peroxidases, enzymes involved in oxidative-stress response. These enzymes are targeted to the interior of encapsulins via unique C-terminal extensions [3]. [1]. 8919789. Nucleotide sequence and taxonomical distribution of the bacteriocin gene lin cloned from Brevibacterium linens M18. Valdes-Stauber N, Scherer S;. Appl Environ Microbiol 1996;62:1283-1286. [2]. 7986050. Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens. Valdes-Stauber N, Scherer S;. Appl Environ Microbiol 1994;60:3809-3814. [3]. 19172747. Structural basis of enzyme encapsulation into a bacterial nanocompartment. Sutter M, Boehringer D, Gutmann S, Gunther S, Prangishvili D, Loessner MJ, Stetter KO, Weber-Ban E, Ban N;. Nat Struct Mol Biol. 2008;15:939-947. (from Pfam)

Date:

2024-10-16

Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide.

Date:

2024-07-04