6x8m
CryoEM structure of the holo-SrpI encapsulin complex from Synechococcus elongatus PCC 7942CryoEM structure of the holo-SrpI encapsulin complex from Synechococcus elongatus PCC 7942
Structural highlights
Publication Abstract from PubMedProkaryotic nanocompartments, also known as encapsulins, are a recently discovered proteinaceous organelle-like compartments in prokaryotes that compartmentalize cargo enzymes. While initial studies have begun to elucidate the structure and physiological roles of encapsulins, bioinformatic evidence suggests that a great diversity of encapsulin nanocompartments remains unexplored. Here, we describe a novel encapsulin in the freshwater cyanobacterium Synechococcus elongatus PCC 7942. This nanocompartment is upregulated upon sulfate starvation and encapsulates a cysteine desulfurase enzyme via an N-terminal targeting sequence. Using cryo-electron microscopy, we have determined the structure of the nanocompartment complex to 2.2 A resolution. Lastly, biochemical characterization of the complex demonstrated that the activity of the cysteine desulfurase is enhanced upon encapsulation. Taken together, our discovery, structural analysis, and enzymatic characterization of this prokaryotic nanocompartment provide a foundation for future studies seeking to understand the physiological role of this encapsulin in various bacteria. Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism.,Nichols RJ, LaFrance B, Phillips NR, Radford DR, Oltrogge LM, Valentin-Alvarado LE, Bischoff AJ, Nogales E, Savage DF Elife. 2021 Apr 6;10. pii: 59288. doi: 10.7554/eLife.59288. PMID:33821786[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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