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Substrate-Induced Conformational Changes in the S-Component ThiT from an Energy Coupling Factor Transporter

Majsnerowska, M., Hänelt, I., Wunnicke, D., Schaefer, L. V., Steinhoff, H-J. & Slotboom, D. J., 7-May-2013, In : Structure. 21, 5, p. 861-867 7 p.

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  • Maria Majsnerowska
  • Inga Hänelt
  • Dorith Wunnicke
  • Lars V. Schaefer
  • Heinz-Juergen Steinhoff
  • Dirk Jan Slotboom

Energy coupling factor (ECF) transporters are a recently discovered class of ABC transporters that mediate vitamin uptake in prokaryotes. Characteristic for ECF-type ABC transporters are small integral membrane proteins (S-components) that bind the transported substrates with high affinity. S-components associate with a second membrane protein (EcfT) and two peripheral ATPases to form a complete ATP-dependent transporter. Here, we have used EPR spectroscopy, stopped-flow fluorescence spectroscopy, and molecular dynamics simulations to determine the structural rearrangements that take place in the S-component ThiT from Lactococcus lactis upon binding of thiamin. Thiamin-induced conformational changes were confined to the long and partially membrane-embedded loop between transmembrane helices 1 and 2 that acts as a lid to occlude the binding site. The results indicate that solitary ThiT functions as a bona fide high-affinity substrate binding protein, which lacks a translocation pathway within the protein.

Original languageEnglish
Pages (from-to)861-867
Number of pages7
JournalStructure
Volume21
Issue number5
Publication statusPublished - 7-May-2013

    Keywords

  • MOLECULAR-DYNAMICS SIMULATIONS, LINEAR CONSTRAINT SOLVER, AMBER FORCE-FIELD, LACTOCOCCUS-LACTIS, ABC TRANSPORTERS, EPR SPECTROSCOPY, BINDING, PROTEINS, PARAMETERS, SYSTEMS

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