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-Structure paper
| Title | Structures of the essential Mycoplasma pneumoniae lipoproteins Mpn444 and Mpn436 reveal a peptidyl-prolyl isomerase domain involved in extracellular protein folding |
|---|---|
| Journal, issue, pages | To Be Published |
| Publish date | Sep 24, 2025 (structure data deposition date) |
Authors | Manger S / Keles I / Frangakis AS / Scheffer MP / Mantanya MS |
External links | Search PubMed |
| Methods | EM (single particle) |
| Resolution | 3.65 - 5.85 Å |
| Structure data | ![]() EMDB-55129: Cryo-EM consensus map (unfocused) of essential Mycoplasma pneumoniae lipoprotein Mpn436 at 3.65 A ![]() EMDB-55131: Cryo-EM focused map of essential Mycoplasma pneumoniae lipoprotein Mpn444 tip region at 4.07 A EMDB-55147: Cryo-EM density map of essential Mycoplasma pneumoniae lipoprotein Mpn444 at 3.74 A EMDB-55148: Cryo-EM density map of essential Mycoplasma pneumoniae lipoprotein Mpn436 at 3.65 A ![]() PDB-9ssc: |
| Source |
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Keywords | CHAPERONE / PPIase Chaperone Mycoplasma pneumoniae lipoprotein |
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mycoplasmoides pneumoniae m129 (bacteria)
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