6a1k
From Proteopedia
Phosphate acyltransferase PlsX from B.subtilis
Structural highlights
Function[PLSX_BACSU] Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.[1] [2] [3] Publication Abstract from PubMedRegions of increased fluidity are newly found bacterial membrane microdomains that are composed of short, unsaturated and branched fatty acyl chains in a fluid and disordered state. Currently, little is known about how proteins are recruited and localized to these membrane domains. Here, we identify a short amphipathic alpha-peptide in a previously unreported crystal structure and show that it is responsible for peripheral localization of the phosphate acyltransferase PlsX to the fluid microdomains in Bacillus subtilis. Mutations disrupting the amphipathic interaction or increasing the nonpolar interaction are found to redistribute the protein to the cytosol or other part of the plasma membrane, causing growth defects. These results reveal a mechanism of peripheral membrane sensing through optimizing nonpolar interaction with the special lipids in the microdomains. This finding shows that the fluid membrane microdomains may take advantage of their unique lipid environment as a means of recruiting and organizing proteins. Identification of an amphipathic peptide sensor of the Bacillus subtilis fluid membrane microdomains.,Jiang Y, Dai X, Qin M, Guo Z Commun Biol. 2019 Aug 20;2:316. doi: 10.1038/s42003-019-0562-8. eCollection 2019. PMID:31453380[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
