MEMBRANE PROTEIN / TYPE-I SECRETION / CELL OUTER MEMBRANE / TRANSPORT / DRUG-EFFLUX
Function / homology
Function and homology information
MacAB-TolC complex / enterobactin transport / bile acid transmembrane transporter activity / xenobiotic detoxification by transmembrane export across the cell outer membrane / efflux pump complex / periplasmic side of plasma membrane / xenobiotic detoxification by transmembrane export across the plasma membrane / bile acid and bile salt transport / porin activity / efflux transmembrane transporter activity ...MacAB-TolC complex / enterobactin transport / bile acid transmembrane transporter activity / xenobiotic detoxification by transmembrane export across the cell outer membrane / efflux pump complex / periplasmic side of plasma membrane / xenobiotic detoxification by transmembrane export across the plasma membrane / bile acid and bile salt transport / porin activity / efflux transmembrane transporter activity / monoatomic ion transmembrane transport / cell outer membrane / response to organic cyclic compound / response to toxic substance / monoatomic ion channel activity / outer membrane-bounded periplasmic space / response to xenobiotic stimulus / response to antibiotic / identical protein binding / membrane Similarity search - Function
Type I secretion outer membrane protein, TolC / Outer membrane efflux proteins (OEP) / Outer membrane efflux proteins (OEP) / Outer membrane efflux protein / Outer membrane efflux protein / Up-down Bundle / Mainly Alpha Similarity search - Domain/homology
SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 13-STRANDED BARREL THIS IS REPRESENTED BY A 14-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
Mass: 18.015 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Formula: H2O
Compound details
ENGINEERED RESIDUE IN CHAIN A, ARG 389 TO SER ENGINEERED RESIDUE IN CHAIN B, ARG 389 TO SER ...ENGINEERED RESIDUE IN CHAIN A, ARG 389 TO SER ENGINEERED RESIDUE IN CHAIN B, ARG 389 TO SER ENGINEERED RESIDUE IN CHAIN C, ARG 389 TO SER
Nonpolymer details
TRIETHYLENE GLYCOL (PGE): FRAGMENT OF PRECIPITANT
Sequence details
V TO L AT GENE POSITION 191 IN ISOLATE USED FOR STRUCTURE DETERMINATION - CORRESPONDS TO L169 IN ...V TO L AT GENE POSITION 191 IN ISOLATE USED FOR STRUCTURE DETERMINATION - CORRESPONDS TO L169 IN THE MATURE FORM OF PROTEIN CRYSTALLIZED
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 4.059 Å3/Da / Density % sol: 69 % / Description: NONE
Crystal grow
pH: 7 Details: 50 MM TRIS PH 8.2, 50 MM NACL, 14% PEG2000, 0.075% N-DODECYL-BETA-D-MALTOSIDE, 0.3% N-OCTYL BETA-D-GLUCOPYRANOSIDE
Resolution: 2.9→29.93 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 2898038.02 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: GEOMETRIC REFINEMENT WAS CARRIED OUT USING CNS VERSION 1.1. B-FACTOR REFINEMENT, BULK SOLVENT MODELLING, AND FINAL R-FACTORS ARE FROM PHENIX. TRIETHYLENE GLYCOL PARAMETER FILE AND TOPOLOGY ...Details: GEOMETRIC REFINEMENT WAS CARRIED OUT USING CNS VERSION 1.1. B-FACTOR REFINEMENT, BULK SOLVENT MODELLING, AND FINAL R-FACTORS ARE FROM PHENIX. TRIETHYLENE GLYCOL PARAMETER FILE AND TOPOLOGY FILE WERE FROM HIC-UP DATABASE.
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