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TitleStructural basis of isethionate transport by a TRAP transporter from a sulfate-reducing bacterium.
Journal, issue, pagesStructure, Vol. 34, Issue 1, Page 133-144.e5, Year 2026
Publish dateJan 8, 2026
AuthorsMichael C Newton-Vesty / Mariafrancesca Scalise / Sam A Jamieson / Michael J Currie / Hamish G Brown / Sepideh Valimehr / Zachary D Tillett / Kelsi R Hall / Senwei Quan / Jane R Allison / Andrew E Whitten / Santosh Panjikar / Cesare Indiveri / Eric Hanssen / Peter D Mace / Rachel A North / Renwick C J Dobson / James S Davies /
PubMed AbstractSulfate-reducing bacteria import organosulfur compounds from the environment for anaerobic respiration. They contribute to human disease and are problematic in industrial settings because they ...Sulfate-reducing bacteria import organosulfur compounds from the environment for anaerobic respiration. They contribute to human disease and are problematic in industrial settings because they produce hydrogen sulfide. Here, we demonstrate how the sulfate-reducing bacterium Oleidesulfovibrio alaskensis imports isethionate, a common organosulfonate, using a tripartite ATP-independent periplasmic (TRAP) transporter (OaIsePQM). The cryo-EM structure of isethionate-bound OaIseQM to 2.98 Å resolution defines the substrate-binding site, two Na-binding sites, and a distinct fusion helix. Key residues within the OaIseQM substrate-binding site are identified using substitution and proteoliposome assays. Functional studies demonstrate that OaIseQM requires the substrate-binding protein (OaIseP) and a Na gradient to drive transport. Modeling of the OaIsePQM complex supports that elevator-type conformational changes are involved in this unique coupled transport process. This work expands our knowledge of the transport of organosulfur compounds in bacteria and establishes OaIsePQM as a new model system for exploring the mechanism of TRAP transporters.
External linksStructure / PubMed:41197622
MethodsEM (single particle)
Resolution2.98 Å
Structure data

EMDB-72036, PDB-9pym:
Cryo-EM structure of the isethionate TRAP transporter IseQM from Oleidesulfovibrio alaskensis with bound isethionate
Method: EM (single particle) / Resolution: 2.98 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-8X3:
2-hydroxyethylsulfonic acid

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • oleidesulfovibrio alaskensis g20 (bacteria)
  • helicobacter pylori (bacteria)
KeywordsTRANSPORT PROTEIN / TRAP Transporter / Megabody / Isethionate

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