RRC ID 30718
Author Kumazaki K, Chiba S, Takemoto M, Furukawa A, Nishiyama K, Sugano Y, Mori T, Dohmae N, Hirata K, Nakada-Nakura Y, Maturana AD, Tanaka Y, Mori H, Sugita Y, Arisaka F, Ito K, Ishitani R, Tsukazaki T, Nureki O.
Title Structural basis of Sec-independent membrane protein insertion by YidC.
Journal Nature
Abstract Newly synthesized membrane proteins must be accurately inserted into the membrane, folded and assembled for proper functioning. The protein YidC inserts its substrates into the membrane, thereby facilitating membrane protein assembly in bacteria; the homologous proteins Oxa1 and Alb3 have the same function in mitochondria and chloroplasts, respectively. In the bacterial cytoplasmic membrane, YidC functions as an independent insertase and a membrane chaperone in cooperation with the translocon SecYEG. Here we present the crystal structure of YidC from Bacillus halodurans, at 2.4 Å resolution. The structure reveals a novel fold, in which five conserved transmembrane helices form a positively charged hydrophilic groove that is open towards both the lipid bilayer and the cytoplasm but closed on the extracellular side. Structure-based in vivo analyses reveal that a conserved arginine residue in the groove is important for the insertion of membrane proteins by YidC. We propose an insertion mechanism for single-spanning membrane proteins, in which the hydrophilic environment generated by the groove recruits the extracellular regions of substrates into the low-dielectric environment of the membrane.
Volume 509(7501)
Pages 516-20
Published 2014-5-22
DOI 10.1038/nature13167
PII nature13167
PMID 24739968
MeSH Arginine / metabolism Bacillus / chemistry* Bacterial Proteins / chemistry* Bacterial Proteins / metabolism* Cell Membrane / chemistry Cell Membrane / metabolism* Conserved Sequence Crystallography, X-Ray Hydrophobic and Hydrophilic Interactions Membrane Transport Proteins / chemistry* Membrane Transport Proteins / metabolism* Molecular Chaperones / chemistry Molecular Chaperones / metabolism Protein Folding Static Electricity Structure-Activity Relationship
IF 42.779
Times Cited 100
DNA material Genomic DNA of Bacillus halodurans JCM 9153 (JGD12232).
General Microbes