Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures of multiple-peptide resistance factor (MprF) from Pseudomonas aeruginosa.
Journal, issue, pages	FEBS J, Year 2026
Publish date	May 22, 2026
Authors	Shaileshanand Jha / Kutti R Vinothkumar /
PubMed Abstract	Aminoacylation of the lipid head group in many bacteria is carried out by bi-functional enzymes called MprF, which encode a soluble synthase domain that typically transfers lysine or alanine from a ...Aminoacylation of the lipid head group in many bacteria is carried out by bi-functional enzymes called MprF, which encode a soluble synthase domain that typically transfers lysine or alanine from a tRNA to lipid head groups. The modified lipid is subsequently translocated across the leaflets by a transmembrane domain. This modification of lipids probably evolved to adapt to the environment where the microbes reside. Here, we describe the cryo-EM structures of MprF enzyme from Pseudomonas aeruginosa, revealing a dimeric enzyme with a distinct architecture when compared with the homologous Rhizobium enzymes, and validate this arrangement with biochemical analyses. The cryo-EM maps and the models in detergent micelle and nanodisc reveal a conformational change of the terminal helix of the synthase domain, highlighting the dynamic elements in the enzyme that might facilitate catalysis. Several lipid-like densities are observed in the cryo-EM maps, which might indicate the path taken by the lipids, coupling the function of the two domains. The structures allow postulation of the binding modes of tRNA and lipid transport, and suggest that the mobile secondary structural elements in the synthase domain might play a mechanistic role in these functions.
External links	FEBS J / PubMed:42175596
Methods	EM (single particle)
Resolution	3.2 - 3.5 Å
Structure data	61238 9j8q EMDB-61238, PDB-9j8q: MprF from Pseudomonas aeruginosa in GDN micelle, C2 symmetry Method: EM (single particle) / Resolution: 3.3 Å 61239 9j8r EMDB-61239, PDB-9j8r: MprF from Pseudomonas aeruginosa in GDN micelle, C1 symmetry Method: EM (single particle) / Resolution: 3.4 Å 61240 9j8s EMDB-61240, PDB-9j8s: MprF from Pseudomonas aeruginosa in nanodisc, C2 symmetry Method: EM (single particle) / Resolution: 3.5 Å 65648 9w50 EMDB-65648, PDB-9w50: MprF from Pseudomonas aeruginosa mutant- H386C/F389C in nanodisc, C2 symmetry Method: EM (single particle) / Resolution: 3.3 Å 65649 9w51 EMDB-65649, PDB-9w51: MprF from Pseudomonas aeruginosa mutant, H566C in nanodisc, C2 symmetry Method: EM (single particle) / Resolution: 3.2 Å
Chemicals	ChemComp-J4U: (2~{R},3~{S},4~{S},5~{S},6~{S})-2-(hydroxymethyl)-6-[(2~{R},3~{S},4~{R},5~{R},6~{R})-2-(hydroxymethyl)-6-[2-[[(2~{R},3~{S},4~{R},5~{R},6~{S})-6-(hydroxymethyl)-5-[(2~{S},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,4-bis(oxidanyl)oxan-2-yl]oxymethyl]-4-[(1~{R},2~{R},4~{S},5'~{R},6~{R},7~{R},8~{R},9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxy-butoxy]-4,5-bis(oxidanyl)oxan-3-yl]oxy-oxane-3,4,5-triol ChemComp-PGT: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipidYM ChemComp-PTY: PHOSPHATIDYLETHANOLAMINE / phospholipidYM
Source	pseudomonas aeruginosa pao1 (bacteria)
Keywords	MEMBRANE PROTEIN / Multiple peptide resistance factor / Membrane Enzyme / Synthase / Flippase / aminoacylated lipid