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Conserved movement of TMS11 between occluded conformations of LacY and XylE of the major facilitator superfamily suggests a similar hinge‐like mechanism
Author(s) -
Västermark Åke,
Driker Adelle,
Li Jiaqi,
Saier Milton H.
Publication year - 2015
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24755
Subject(s) - major facilitator superfamily , superfamily , transmembrane domain , movement (music) , crystallography , biophysics , terminal (telecommunication) , geometry , linker , anatomy , computer science , biology , chemistry , physics , mathematics , biochemistry , amino acid , transporter , telecommunications , acoustics , gene , operating system
The Δ‐distance maps can detect local remodeling that is difficult to accurately determine using superimpositions. Transmembrane segments (TMSs) 11 in both LacY and XylE of the major facilitator superfamily uniquely contribute the greatest amount of mobile surface area in the outward‐occluded state and undergo analogous movements. The intracellular part of TMS11 moves away from the C ‐terminal domain and into the substrate cavity during the conformational change from the outward‐occluded to the inward‐occluded state. A difference was noted between LacY and XylE when they assumed the inward open state after releasing a substrate to the inside in which TMS11 of LacY moved further into the substrate release space, whereas in XylE, TMS11 slightly retracted into the C ‐terminal domain. Independent movement of the N ‐terminal half of TMS11 suggests that it is flexible in the middle. Repeat‐swapped homology modeling was used to discover that a loop connecting TMSs 10 and 11 in LacY probably moves during the transition between the unavailable outward‐open state and the outward‐occluded state. TMSs 11 and the other elements displaying a notable domain‐independent movement colocalize with the interdomain linker, suggesting that these elements could drive the alternating access movement between the domain halves. Preliminary evidence indicates that analogous movements occur in other members of the major facilitator superfamily. Proteins 2015; 83:735–745. © 2015 Wiley Periodicals, Inc.