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NYU Dataset
Structural Basis of Ion-Substrate Coupling in the Sodium-Dependent Dicarboxylate Transporter VcINDY
- Authors
- David B. SauerJennifer J. MardenJoseph C. SudarJinmei Song2 more author(s)...
- Description
VcINDY is a sodium-dependent dicarboxylate transporter that imports tricarboxylic acid cycle intermediates across the inner membrane of Vibrio cholerae. This study used a combination of structure determination by single-particle cryo-electron microscopy, substrate-binding affinity measurements by intrinsic tryptophan fluorescence quenching, and position accessibility quantification by site-directed...
- Subject
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Proteomics
- Access Rights
- Free to All
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NYU Dataset
Energy Coupling and Stoichiometry of Zn2+/H+ Antiport by YiiP
- Authors
- Adel HusseinShujie FanMaria Lopez-RedondoIan Kenney3 more author(s)...
- Description
Previous studies of YiiP, bacterial Zn2+/H+ antiporter, have shown a homodimeric architecture and the presence of three distinct Zn2+ binding sites. YiiP is a representative of the cation diffusion facilitator superfamily, which are responsible for homeostasis of transition metal ions. This study used cryo-electron microscopy, microscale thermophoresis, and molecular dynamics simulations to address...
- Subject
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Proteomics
- Access Rights
- Free to All
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NYU Dataset
Substrate Translocation and Inhibition in Human Dicarboxylate Transporter NaDC3
- Authors
- Yan LiJinmei SongVedrana MikusevicJennifer J. Marden6 more author(s)...
- Description
High-affinity sodium–dicarboxylate cotransporter (NaDC3) imports various substrates into the cell as tricarboxylate acid cycle intermediates, lipid biosynthesis precursors, and signaling molecules. To understand the cellular signaling process and developing inhibitors requires knowledge of the structural basis of the dicarboxylate specificity and inhibition mechanism of NaDC3. This study used single-particle...
- Subject
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Proteomics
- Access Rights
- Free to All
