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TitlePhospholipid translocation captured in a bifunctional membrane protein MprF.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 2927, Year 2021
Publish dateMay 18, 2021
AuthorsDanfeng Song / Haizhan Jiao / Zhenfeng Liu /
PubMed AbstractAs a large family of membrane proteins crucial for bacterial physiology and virulence, the Multiple Peptide Resistance Factors (MprFs) utilize two separate domains to synthesize and translocate ...As a large family of membrane proteins crucial for bacterial physiology and virulence, the Multiple Peptide Resistance Factors (MprFs) utilize two separate domains to synthesize and translocate aminoacyl phospholipids to the outer leaflets of bacterial membranes. The function of MprFs enables Staphylococcus aureus and other pathogenic bacteria to acquire resistance to daptomycin and cationic antimicrobial peptides. Here we present cryo-electron microscopy structures of MprF homodimer from Rhizobium tropici (RtMprF) at two different states in complex with lysyl-phosphatidylglycerol (LysPG). RtMprF contains a membrane-embedded lipid-flippase domain with two deep cavities opening toward the inner and outer leaflets of the membrane respectively. Intriguingly, a hook-shaped LysPG molecule is trapped inside the inner cavity with its head group bent toward the outer cavity which hosts a second phospholipid-binding site. Moreover, RtMprF exhibits multiple conformational states with the synthase domain adopting distinct positions relative to the flippase domain. Our results provide a detailed framework for understanding the mechanisms of MprF-mediated modification and translocation of phospholipids.
External linksNat Commun / PubMed:34006869 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.998 - 3.7 Å
Structure data

0992

6lvf

EMDB-0992, PDB-6lvf:
Cryo-EM structure of the multiple peptide resistance factor (MprF) loaded with one lysyl-phosphatidylglycerol molecule
Method: EM (single particle) / Resolution: 3.7 Å

30869

7duw

EMDB-30869, PDB-7duw:
Cryo-EM structure of the multiple peptide resistance factor (MprF) loaded with two lysyl-phosphatidylglycerol molecules
Method: EM (single particle) / Resolution: 2.96 Å

PDB-6lv0:
Crystal structure of the soluble domain of the multiple peptide resistance factor (MprF) from Rhizobium tropici
Method: X-RAY DIFFRACTION / Resolution: 1.998 Å

Chemicals

ChemComp-HOH:
WATER / Water

ChemComp-EV9:
[(2~{R})-3-[[(2~{S})-3-[(2~{S})-2,6-bis(azanyl)hexanoyl]oxy-2-oxidanyl-propoxy]-oxidanyl-phosphoryl]oxy-2-hexadecanoyloxy-propyl] hexadecanoate

ChemComp-LHG:
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipid*YM / Phosphatidylglycerol

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM / Phosphatidylglycerol

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

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

Source
  • rhizobium tropici (bacteria)
  • rhizobium tropici ciat 899 (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / lipid biosynthesis / MEMBRANE PROTEIN / bacteria membrane protein

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