Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7WAG

Crystal structure of MurJ squeezed form

Summary for 7WAG
Entry DOI10.2210/pdb7wag/pdb
DescriptorLipid II flippase MurJ, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
Functional Keywords14 transmembrane helices, inner membrane, lipid ii, mop superfamily, lipid transport
Biological sourceEscherichia coli K-12
Total number of polymer chains1
Total formula weight61320.55
Authors
Tsukazaki, T.,Kohga, H.,Tanaka, Y.,Yoshikaie, K.,Taniguchi, K.,Fujimoto, K. (deposition date: 2021-12-14, release date: 2022-06-01, Last modification date: 2023-11-29)
Primary citationKohga, H.,Mori, T.,Tanaka, Y.,Yoshikaie, K.,Taniguchi, K.,Fujimoto, K.,Fritz, L.,Schneider, T.,Tsukazaki, T.
Crystal structure of the lipid flippase MurJ in a "squeezed" form distinct from its inward- and outward-facing forms.
Structure, 30:1088-1097.e3, 2022
Cited by
PubMed Abstract: The bacterial peptidoglycan enclosing the cytoplasmic membrane is a fundamental cellular architecture. The integral membrane protein MurJ plays an essential role in flipping the cell wall building block Lipid II across the cytoplasmic membrane for peptidoglycan biosynthesis. Previously reported crystal structures of MurJ have elucidated its V-shaped inward- or outward-facing forms with an internal cavity for substrate binding. MurJ transports Lipid II using its cavity through conformational transitions between these two forms. Here, we report two crystal structures of inward-facing forms from Arsenophonus endosymbiont MurJ and an unprecedented crystal structure of Escherichia coli MurJ in a "squeezed" form, which lacks a cavity to accommodate the substrate, mainly because of the increased proximity of transmembrane helices 2 and 8. Subsequent molecular dynamics simulations supported the hypothesis that the squeezed form is an intermediate conformation. This study fills a gap in our understanding of the Lipid II flipping mechanism.
PubMed: 35660157
DOI: 10.1016/j.str.2022.05.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.55 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon