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7VR6

Crystal structure of MlaC from Escherichia coli in quasi-open state

Summary for 7VR6
Entry DOI10.2210/pdb7vr6/pdb
DescriptorIntermembrane phospholipid transport system binding protein MlaC, DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsabc transporter, periplasmic protein, membrane lipid asymmetry, segmented domain movement, mla transport system, transport protein
Biological sourceEscherichia coli K-12
Total number of polymer chains1
Total formula weight23471.79
Authors
Dutta, A.,Kanaujia, S.P. (deposition date: 2021-10-21, release date: 2022-09-21, Last modification date: 2023-11-29)
Primary citationDutta, 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: 36084896
DOI: 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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