7DUW
Cryo-EM structure of the multiple peptide resistance factor (MprF) loaded with two lysyl-phosphatidylglycerol molecules
Summary for 7DUW
| Entry DOI | 10.2210/pdb7duw/pdb |
| EMDB information | 0992 30869 |
| Descriptor | Bifunctional lysylphosphatidylglycerol flippase/synthetase MprF, DODECYL-BETA-D-MALTOSIDE, [(2~{R})-3-[[(2~{S})-3-[(2~{S})-2,6-bis(azanyl)hexanoyl]oxy-2-oxidanyl-propoxy]-oxidanyl-phosphoryl]oxy-2-hexadecanoyloxy-propyl] hexadecanoate, ... (7 entities in total) |
| Functional Keywords | bacteria membrane protein, membrane protein |
| Biological source | Rhizobium tropici |
| Total number of polymer chains | 2 |
| Total formula weight | 201893.76 |
| Authors | Song, D.F.,Jiao, H.Z.,Liu, Z.F. (deposition date: 2021-01-12, release date: 2021-04-21, Last modification date: 2024-06-05) |
| Primary citation | Song, D.,Jiao, H.,Liu, Z. Phospholipid translocation captured in a bifunctional membrane protein MprF. Nat Commun, 12:2927-2927, 2021 Cited by PubMed Abstract: 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. PubMed: 34006869DOI: 10.1038/s41467-021-23248-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.96 Å) |
Structure validation
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