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#bacterial transport

4 public questions tagged with this topic.

Lactose permease functions as a:

Lactose permease LacY of Escherichia coli, characterized extensively by Kaback, is a twelve-transmembrane helix member of major facilitator superfamily and textbook exemplar of secondary active symport. LacY itself does not possess ATPase activity nor nucleoside-binding motifs; energy comes indirectly from electrochemical proton gradient across inner membrane maintained by respiratory chain H+ extrusion. In outward-open state protonation of Glu325 increases affinity for lactose at the central cavity; coupled binding induces rocker-switch movement of N and C terminal six-helix bundles to inward

Ref: Kaback et al., Nat Rev Mol Cell Biol 2001, LacY mechanism; Alberts, Chapter 11 carriers.

The Porin proteins in Gram-negative bacteria facilitate:

In Gram-negative organisms, outer membrane asymmetry places lipopolysaccharide in outer leaflet and phospholipid inside, rendering it intrinsically impermeable to many hydrophilic compounds, including bile salts and antibiotics like vancomycin. Nutrient acquisition therefore depends on abundant trimeric beta-barrel proteins known as porins, exemplified by general porins OmpF, OmpC, and PhoE in Escherichia coli. Each monomer folds as a 16-stranded antiparallel barrel creating a water-filled channel lined with charged residues forming eyelet constriction that determines size exclusion near 600 d

Ref: Alberts et al., Molecular Biology Cell, 7th ed., Chapter 10: Porins; Delcour, Biochim Biophys Acta 2009, Outer Membrane Permeability.

Function of lactose permease is

Lactose permease functions through classical alternating-access transport mechanism: outward-open conformation binds extracellular lactose plus proton on specific side chains, undergoes conformational change to occluded state, then rearranges to inward-open releasing substrates into cytoplasm. Proton coupling utilizes electrochemical gradient across inner membrane to drive accumulation to concentrations hundredfold higher than environment even when external lactose remains micromolar. Influx supplies beta-galactosidase substrate producing glucose, galactose, and allolactose inducer driving fur

Ref: Wikipedia Lactose permease – LacY proton symport transports lactose using proton gradient, increasing cell permeability.

lacY gene product is

lacY gene product is lactose permease LacY, 417-residue member of major facilitator superfamily transporter folded into twelve transmembrane alpha helices forming central hydrophilic cavity accessible alternately outward and inward during cycle. It operates as galactoside-proton symporter driven entirely by proton motive force, accumulating lactose against concentration gradient for metabolic use. Protein functionality is distinct from soluble beta-galactosidase encoded by lacZ and transacetylase LacA. By concentrating intracellular beta-galactosides, LacY enables efficient generation of allol

Ref: ScienceDirect Lactose Permease overview – LacY transmembrane symporter concentrates β-galactosides for hydrolysis and induction.