7VR6
Crystal structure of MlaC from Escherichia coli in quasi-open state
Summary for 7VR6
Entry DOI | 10.2210/pdb7vr6/pdb |
Descriptor | Intermembrane phospholipid transport system binding protein MlaC, DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | abc transporter, periplasmic protein, membrane lipid asymmetry, segmented domain movement, mla transport system, transport protein |
Biological source | Escherichia coli K-12 |
Total number of polymer chains | 1 |
Total formula weight | 23471.79 |
Authors | Dutta, A.,Kanaujia, S.P. (deposition date: 2021-10-21, release date: 2022-09-21, Last modification date: 2023-11-29) |
Primary citation | Dutta, A.,Prasad Kanaujia, S. MlaC belongs to a unique class of non-canonical substrate-binding proteins and follows a novel phospholipid-binding mechanism. J.Struct.Biol., 214:107896-107896, 2022 Cited by PubMed: 36084896DOI: 10.1016/j.jsb.2022.107896 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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