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TitleMobile barrier mechanisms for Na-coupled symport in an MFS sugar transporter.
Journal, issue, pagesElife, Vol. 12, Year 2024
Publish dateFeb 21, 2024
AuthorsParameswaran Hariharan / Yuqi Shi / Satoshi Katsube / Katleen Willibal / Nathan D Burrows / Patrick Mitchell / Amirhossein Bakhtiiari / Samantha Stanfield / Els Pardon / H Ronald Kaback / Ruibin Liang / Jan Steyaert / Rosa Viner / Lan Guan /
PubMed AbstractWhile many 3D structures of cation-coupled transporters have been determined, the mechanistic details governing the obligatory coupling and functional regulations still remain elusive. The bacterial ...While many 3D structures of cation-coupled transporters have been determined, the mechanistic details governing the obligatory coupling and functional regulations still remain elusive. The bacterial melibiose transporter (MelB) is a prototype of major facilitator superfamily transporters. With a conformation-selective nanobody, we determined a low-sugar affinity inward-facing Na-bound cryoEM structure. The available outward-facing sugar-bound structures showed that the N- and C-terminal residues of the inner barrier contribute to the sugar selectivity. The inward-open conformation shows that the sugar selectivity pocket is also broken when the inner barrier is broken. Isothermal titration calorimetry measurements revealed that this inward-facing conformation trapped by this nanobody exhibited a greatly decreased sugar-binding affinity, suggesting the mechanisms for substrate intracellular release and accumulation. While the inner/outer barrier shift directly regulates the sugar-binding affinity, it has little or no effect on the cation binding, which is supported by molecular dynamics simulations. Furthermore, the hydron/deuterium exchange mass spectrometry analyses allowed us to identify dynamic regions; some regions are involved in the functionally important inner barrier-specific salt-bridge network, which indicates their critical roles in the barrier switching mechanisms for transport. These complementary results provided structural and dynamic insights into the mobile barrier mechanism for cation-coupled symport.
External linksElife / PubMed:38381130 / PubMed Central
MethodsEM (single particle)
Resolution3.29 Å
Structure data

41062

8t60

EMDB-41062, PDB-8t60:
CryoEM structure of an inward-facing MelBSt at a Na(+)-bound and sugar low-affinity conformation
Method: EM (single particle) / Resolution: 3.29 Å

Chemicals

ChemComp-NA:
Unknown entry

Source
  • Escherichia coli (E. coli)
  • salmonella enterica subsp. enterica serovar typhimurium (bacteria)
  • synthetic construct (others)
KeywordsTRANSPORT PROTEIN / Sugar transporter; Cation-coupled symporter; Na(+) binding; Protein conformation; Nanobodies; NabFab; CryoEM / Membrane proteins; protein-protein interaction

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