7MBZ
Outward facing conformation of the MetNI methionine ABC transporter in complex with lipo-MetQ
Summary for 7MBZ
Entry DOI | 10.2210/pdb7mbz/pdb |
EMDB information | 23751 |
Descriptor | ABC transporter, permease protein, Lipoprotein, ABC transporter, ATP-binding protein (3 entities in total) |
Functional Keywords | membrane protein |
Biological source | Neisseria meningitidis serogroup B (strain MC58) More |
Total number of polymer chains | 5 |
Total formula weight | 141468.68 |
Authors | Sharaf, N.G.,Rees, D.C. (deposition date: 2021-04-01, release date: 2021-09-01, Last modification date: 2024-05-29) |
Primary citation | Sharaf, N.G.,Shahgholi, M.,Kim, E.,Lai, J.Y.,VanderVelde, D.G.,Lee, A.T.,Rees, D.C. Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction. Elife, 10:-, 2021 Cited by PubMed: 34409939DOI: 10.7554/eLife.69742 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (6.4 Å) |
Structure validation
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