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  • Title: The structural basis of modularity in ECF-type ABC transporters.
    Author: Erkens GB, Berntsson RP, Fulyani F, Majsnerowska M, Vujičić-Žagar A, Ter Beek J, Poolman B, Slotboom DJ.
    Journal: Nat Struct Mol Biol; 2011 Jun 26; 18(7):755-60. PubMed ID: 21706007.
    Abstract:
    Energy coupling factor (ECF) transporters are used for the uptake of vitamins in Prokarya. They consist of an integral membrane protein that confers substrate specificity (the S-component) and an energizing module that is related to ATP-binding cassette (ABC) transporters. S-components for different substrates often do not share detectable sequence similarity but interact with the same energizing module. Here we present the crystal structure of the thiamine-specific S-component ThiT from Lactococcus lactis at 2.0 Å. Extensive protein-substrate interactions explain its high binding affinity for thiamine (K(d) ~10(-10) M). ThiT has a fold similar to that of the riboflavin-specific S-component RibU, with which it shares only 14% sequence identity. Two alanines in a conserved motif (AxxxA) located on the membrane-embedded surface of the S-components mediate the interaction with the energizing module. Based on these findings, we propose a general transport mechanism for ECF transporters.
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