5UL9

Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant

Summary for 5UL9

• Entry DOI: 10.2210/pdb5ul9/pdb
• Related: 5UL7 5ULD 5ULE
• Descriptor: Transporter, NadC family, SODIUM ION, CITRIC ACID (3 entities in total)
• Functional Keywords: transport protein
• Biological source: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
• Total number of polymer chains: 4
• Total formula weight: 191103.07

Authors

Lu, M. (deposition date: 2017-01-24, release date: 2017-05-17, Last modification date: 2024-03-06)

Primary citation

Nie, R.,Stark, S.,Symersky, J.,Kaplan, R.S.,Lu, M.
Structure and function of the divalent anion/Na(+) symporter from Vibrio cholerae and a humanized variant.
Nat Commun, 8:15009-15009, 2017

PubMed Abstract: Integral membrane proteins of the divalent anion/Na symporter (DASS) family translocate dicarboxylate, tricarboxylate or sulphate across cell membranes, typically by utilizing the preexisting Na gradient. The molecular determinants for substrate recognition by DASS remain obscure, largely owing to the absence of any substrate-bound DASS structure. Here we present 2.8-Å resolution X-ray structures of VcINDY, a DASS from Vibrio cholerae that catalyses the co-transport of Na and succinate. These structures portray the Na-bound VcINDY in complexes with succinate and citrate, elucidating the binding sites for substrate and two Na ions. Furthermore, we report the structures of a humanized variant of VcINDY in complexes with succinate and citrate, which predict how a human citrate-transporting DASS may interact with its bound substrate. Our findings provide insights into metabolite transport by DASS, establishing a molecular basis for future studies on the regulation of this transport process.

PubMed: 28436435
DOI: 10.1038/ncomms15009

Experimental method

X-RAY DIFFRACTION (2.78 Å)