6A1K

Phosphate acyltransferase PlsX from B.subtilis

Summary for 6A1K

• Entry DOI: 10.2210/pdb6a1k/pdb
• Descriptor: Phosphate acyltransferase, SULFATE ION (3 entities in total)
• Functional Keywords: phosphate acyltransferase, transferase
• Biological source: Bacillus subtilis subsp. subtilis str. 168
• Total number of polymer chains: 2
• Total formula weight: 72224.68

Authors

Guo, Z.,Jiang, Y. (deposition date: 2018-06-07, release date: 2019-06-12, Last modification date: 2024-03-27)

Primary citation

Jiang, Y.,Dai, X.,Qin, M.,Guo, Z.
Identification of an amphipathic peptide sensor of the Bacillus subtilisfluid membrane microdomains.
Commun Biol, 2:316-316, 2019

PubMed Abstract: Regions 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 α-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 . 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.

PubMed: 31453380
DOI: 10.1038/s42003-019-0562-8

Experimental method

X-RAY DIFFRACTION (2.3 Å)