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Yorodumi- PDB-7duw: Cryo-EM structure of the multiple peptide resistance factor (MprF... -
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Entry | Database: PDB / ID: 7duw | ||||||||||||
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Title | Cryo-EM structure of the multiple peptide resistance factor (MprF) loaded with two lysyl-phosphatidylglycerol molecules | ||||||||||||
Components | Bifunctional lysylphosphatidylglycerol flippase/synthetase MprF | ||||||||||||
Keywords | MEMBRANE PROTEIN / bacteria membrane protein | ||||||||||||
Function / homology | Function and homology information phosphatidylglycerol alanyltransferase activity / phospholipid homeostasis / plasma membrane Similarity search - Function | ||||||||||||
Biological species | Rhizobium tropici (bacteria) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.96 Å | ||||||||||||
Authors | Song, D.F. / Jiao, H.Z. / Liu, Z.F. | ||||||||||||
Funding support | China, 3items
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Citation | Journal: Nat Commun / Year: 2021 Title: Phospholipid translocation captured in a bifunctional membrane protein MprF. Authors: Danfeng Song / Haizhan Jiao / Zhenfeng Liu / 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 ...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. | ||||||||||||
History |
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-Structure visualization
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Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 7duw.cif.gz | 305.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7duw.ent.gz | 243.9 KB | Display | PDB format |
PDBx/mmJSON format | 7duw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7duw_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 7duw_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 7duw_validation.xml.gz | 62.2 KB | Display | |
Data in CIF | 7duw_validation.cif.gz | 87.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/du/7duw ftp://data.pdbj.org/pub/pdb/validation_reports/du/7duw | HTTPS FTP |
-Related structure data
Related structure data | 30869MC 0992C 6lv0C 6lvfC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data |
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Deposited unit |
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-Components
-Protein / Sugars , 2 types, 4 molecules AB
#1: Protein | Mass: 96094.672 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rhizobium tropici (bacteria) / Gene: mprF, GXW80_12690 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A6P1C618 #2: Sugar | |
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-Non-polymers , 5 types, 12 molecules
#3: Chemical | ChemComp-EV9 / [( #4: Chemical | #5: Chemical | #6: Chemical | |
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