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

MlaC belongs to a unique class of non-canonical substrate-binding proteins and follows a novel phospholipid-binding mechanism.

Intermembrane phospholipid transport system binding protein MlaC

MHHHHHHADQTNPYKLMDEAAQKTFDRLKNEQPQIRANPDYLRTIVDQELLPYVQVKYAGALVLGQYYKSATPAQREAYF
AAFREYLKQAYGQALAMYHGQTYQIAPEQPLGDKTIVPIRVTIIDPNGRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMI
TTKQNEWGTLLRTKGIDGLTAQLKSISQQKITLEEKK

THE ENTRY CONTAINS FRIEDEL PAIRS IN I/F_PLUS/MINUS COLUMNS.

0.7 M sodium citrate tribasic dihydrate, 0.1 M Bis-Tris propane pH 7.0

Science and Engineering Research Board (SERB)

U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

ABC transporter, Periplasmic protein, Membrane lipid asymmetry, Segmented domain movement, Mla transport system, TRANSPORT PROTEIN

ADQTNPYKLMDEAAQKTFDRLKNEQPQIRANPDYLRTIVDQELLPYVQVKYAGALVLGQYYKSATPAQREAYFAAFREYL
KQAYGQALAMYHGQTYQIAPEQPLGDKTIVPIRVTIIDPNGRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMITTKQNEW
GTLLRTKGIDGLTAQLKSISQQKITLEEKK