3dkt
Crystal structure of Thermotoga maritima encapsulinCrystal structure of Thermotoga maritima encapsulin
Structural highlights
Function[MARIT_THEMA] Protease that exhibits activity toward chymotrypsin and trypsin substrates. May have antibacterial activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCompartmentalization is an important organizational feature of life. It occurs at varying levels of complexity ranging from eukaryotic organelles and the bacterial microcompartments, to the molecular reaction chambers formed by enzyme assemblies. The structural basis of enzyme encapsulation in molecular compartments is poorly understood. Here we show, using X-ray crystallographic, biochemical and EM experiments, that a widespread family of conserved bacterial proteins, the linocin-like proteins, form large assemblies that function as a minimal compartment to package enzymes. We refer to this shell-forming protein as 'encapsulin'. The crystal structure of such a particle from Thermotoga maritima determined at 3.1-angstroms resolution reveals that 60 copies of the monomer assemble into a thin, icosahedral shell with a diameter of 240 angstroms. The interior of this nanocompartment is lined with conserved binding sites for short polypeptide tags present as C-terminal extensions of enzymes involved in oxidative-stress response. 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 Sep;15(9):939-47. PMID:19172747[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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