ArticleProceedings of the National Academy of Sciences of the United States of America2012
Evidence for an intermediate conformational state of LacY.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- The proton electrochemical gradient induces a kinetic asymmetry in the symport cycle of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The lipid-dependent structure and function of LacY can be recapitulated and analyzed in phospholipid-containing detergent micelles.Scientific reports · 2019Article
- Crystal structure of a LacY-nanobody complex in a periplasmic-open conformation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Role of Conserved Gly-Gly Pairs on the Periplasmic Side of LacY.Biochemistry · 2016Article
- Dynamic membrane protein topological switching upon changes in phospholipid environment.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Effect of Detergents on Galactoside Binding by Melibiose Permeases.Biochemistry · 2015Article
- A chemiosmotic mechanism of symport.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Membrane proteins, detergents and crystals: what is the state of the art?Acta crystallographica. Section F, Structural biology communications · 2014Review
- Article
- Functional architecture of MFS D-glucose transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Understanding transporter specificity and the discrete appearance of channel-like gating domains in transporters.Frontiers in pharmacology · 2014Review
- The periplasmic cavity of LacY mutant Cys154→Gly: how open is open?Biochemistry · 2013Article
- Article
- Trp replacements for tightly interacting Gly-Gly pairs in LacY stabilize an outward-facing conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Apo-intermediate in the transport cycle of lactose permease (LacY).Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Dynamics of the L-fucose/H+ symporter revealed by fluorescence spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Role of the irreplaceable residues in the LacY alternating access mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
LacY mutant Cys154 → Gly exhibits a periplasmic-closed crystal structure identical to the WT, but is periplasmic-open in the membrane. The mutant hardly catalyzes transport, but binds galactosides from either side of the membrane with the same affinity and is resistant to site-directed proteolysis relative to the pseudo-WT. Site-directed alkylation was also applied to 11 single-Cys mutants in Cys154 → Gly LacY in right-side-out membrane vesicles or after solubilization and purification in dodecyl-β-D-maltopyranoside (DDM). Unlike the pseudo-WT, Cys replacements on the periplasmic side of the Cys154 → Gly mutant label rapidly in the membrane without sugar, but labeling decreases markedly after the mutant proteins are purified. Thus, Cys154 → Gly LacY likely favors a higher-energy intermediate periplasmic-open conformation in situ, but collapses to a lower-energy periplasmic-closed conformation in DDM after purification. Notably, branched-chain or neopentyl glycol maltoside detergents stabilize Cys154 → Gly LacY in the membrane-embedded form.
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