Crystal structure of MlaC from Escherichia coli in quasi-open state. Determined by X-ray diffraction at 2.5 Å resolution. Released 21 Sept 2022.
Explore 7VR6 in 3D Show helices and sheets RCSB PDB PDBe
7VR6 contains 11 α-helices and 6 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-44 | 18 | |
| α-helix | 46-51 | 6 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-63 | 8 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68 | 1 | 1 |
| α-helix | 70-78 | 9 | |
| α-helix | 79-82 | 4 | |
| α-helix | 87-109 | 23 | |
| β-strand | 116-119 | 4 | 1 |
| β-strand | 130-138 | 9 | 1 |
| α-helix | 143-145 | 3 | |
| β-strand | 146-154 | 9 | 1 |
| β-strand | 161-168 | 8 | 1 |
| β-strand | 171-172 | 2 | 1 |
| α-helix | 173-201 | 29 | |
| α-helix | 204-205 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Intermembrane phospholipid transport system binding protein MlaC | A | protein | 197 | Escherichia coli K-12 | P0ADV7 (AlphaFold model) |
>7VR6_1 Intermembrane phospholipid transport system binding protein MlaC (chains A) MHHHHHHADQTNPYKLMDEAAQKTFDRLKNEQPQIRANPDYLRTIVDQELLPYVQVKYAG ALVLGQYYKSATPAQREAYFAAFREYLKQAYGQALAMYHGQTYQIAPEQPLGDKTIVPIR VTIIDPNGRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMITTKQNEWGTLLRTKGIDGLT AQLKSISQQKITLEEKK
| ID | Name | Formula | Copies |
|---|---|---|---|
| PEF | Di-palmitoyl-3-sn-phosphatidylethanolamine | C37 H74 N O8 P | 1 |
Water and common crystallization additives (EDO) are not listed.
MlaC belongs to a unique class of non-canonical substrate-binding proteins and follows a novel phospholipid-binding mechanism. Dutta, A., Prasad Kanaujia, S. J Struct Biol (2022) 214:107896-107896. DOI 10.1016/j.jsb.2022.107896 · PubMed
Other PDB entries of the same protein (UniProt P0ADV7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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