Major Facilitator Superfamily Porters, LacY, FucP and XylE of <b><i>Escherichia coli</i></b> Appear to Have Evolved Positionally Dissimilar Catalytic Residues without Rearrangement of 3-TMS Repeat Units

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Major facilitator superfamily porters, LacY, FucP and XylE of Escherichia coli appear to have evolved positionally dissimilar catalytic residues without rearrangement of 3-TMS repeat units.

Based on alleged functional residue correspondences between FucP and LacY, a recent study has resulted in a proposed model of 3-TMS unit rearrangements [Madej et al.: Proc Natl Acad Sci USA 2013;110:5870-5874]. We rebut this theory, using 7 different lines of evidence. Our observations suggest that these two transporters are homologous throughout their lengths, having evolved from a common ance...

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Major Facilitator Superfamily (MFS) evolved without 3-transmembrane segment unit rearrangements.

Based on alleged functional residue correspondences, a recent study proposed a model of 3-transmembrane segment (TMS) repeat unit rearrangements in Major Facilitator Superfamily (MFS) carriers (1). A rebuttal of “Evolutionary mix-and-match with MFS transporters” (1) is currently in press in the Journal of Molecular Microbiology and Biotechnology (2). In their follow-up paper, “Evolutionary mix-...

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Major facilitator superfamily.

The major facilitator superfamily (MFS) is one of the two largest families of membrane transporters found on Earth. It is present ubiquitously in bacteria, archaea, and eukarya and includes members that can function by solute uniport, solute/cation symport, solute/cation antiport and/or solute/solute antiport with inwardly and/or outwardly directed polarity. All homologous MFS protein sequences...

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Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE

The major facilitator superfamily (MFS) is the largest collection of structurally related membrane proteins that transport a wide array of substrates. The proton-coupled sugar transporter XylE is the first member of the MFS that has been structurally characterized in multiple transporting conformations, including both the outward and inward-facing states. Here we report the crystal structure of...

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Integration of Evolutionary Features for the Identification of Functionally Important Residues in Major Facilitator Superfamily Transporters

The identification of functionally important residues is an important challenge for understanding the molecular mechanisms of proteins. Membrane protein transporters operate two-state allosteric conformational changes using functionally important cooperative residues that mediate long-range communication from the substrate binding site to the translocation pathway. In this study, we identified ...

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ژورنال

عنوان ژورنال: Journal of Molecular Microbiology and Biotechnology

سال: 2014

ISSN: 1464-1801,1660-2412

DOI: 10.1159/000358429