Arg302 governs the pKa of Glu325 in LacY

Proceedings of the National Academy of Sciences of the United States of America
Natalia GrytsykPetra Hellwig

Abstract

Lactose permease is a paradigm for the major facilitator superfamily, the largest family of ion-coupled membrane transport proteins known at present. LacY carries out the coupled stoichiometric symport of a galactoside with an H+, using the free energy released from downhill translocation of H+ to drive accumulation of galactosides against a concentration gradient. In neutrophilic Escherichia coli, internal pH is kept at ∼7.6 over the physiological range, but the apparent pK (pKapp) for galactoside binding is 10.5. Surface-enhanced infrared absorption spectroscopy (SEIRAS) demonstrates that the high pKa is due to Glu325 (helix X), which must be protonated for LacY to bind galactoside effectively. Deprotonation is also obligatory for turnover, however. Here, we utilize SEIRAS to study the effect of mutating residues in the immediate vicinity of Glu325 on its pKa The results are consistent with the idea that Arg302 (helix IX) is important for deprotonation of Glu325.

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Feb 6, 2017·Proceedings of the National Academy of Sciences of the United States of America·Natalia GrytsykPetra Hellwig

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Citations

May 31, 2019·The Journal of General Physiology·H Ronald Kaback, Lan Guan
Jan 1, 2020·Proceedings of the National Academy of Sciences of the United States of America·Xiaoxu JiangH Ronald Kaback
Aug 30, 2020·The Journal of Biological Chemistry·Ana Filipa Santos SeicaPetra Hellwig
Mar 24, 2020·Chemical Reviews·Victor A Lorenz-Fonfria
Mar 22, 2021·The Journal of Biological Chemistry·Fei LiRobert M Stroud

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