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TitleStructural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 4471, Year 2022
Publish dateAug 4, 2022
AuthorsMartin F Peter / Jan A Ruland / Peer Depping / Niels Schneberger / Emmanuele Severi / Jonas Moecking / Karl Gatterdam / Sarah Tindall / Alexandre Durand / Veronika Heinz / Jan Peter Siebrasse / Paul-Albert Koenig / Matthias Geyer / Christine Ziegler / Ulrich Kubitscheck / Gavin H Thomas / Gregor Hagelueken /
PubMed AbstractTripartite ATP-independent periplasmic (TRAP) transporters are found widely in bacteria and archaea and consist of three structural domains, a soluble substrate-binding protein (P-domain), and two ...Tripartite ATP-independent periplasmic (TRAP) transporters are found widely in bacteria and archaea and consist of three structural domains, a soluble substrate-binding protein (P-domain), and two transmembrane domains (Q- and M-domains). HiSiaPQM and its homologs are TRAP transporters for sialic acid and are essential for host colonization by pathogenic bacteria. Here, we reconstitute HiSiaQM into lipid nanodiscs and use cryo-EM to reveal the structure of a TRAP transporter. It is composed of 16 transmembrane helices that are unexpectedly structurally related to multimeric elevator-type transporters. The idiosyncratic Q-domain of TRAP transporters enables the formation of a monomeric elevator architecture. A model of the tripartite PQM complex is experimentally validated and reveals the coupling of the substrate-binding protein to the transporter domains. We use single-molecule total internal reflection fluorescence (TIRF) microscopy in solid-supported lipid bilayers and surface plasmon resonance to study the formation of the tripartite complex and to investigate the impact of interface mutants. Furthermore, we characterize high-affinity single variable domains on heavy chain (VHH) antibodies that bind to the periplasmic side of HiSiaQM and inhibit sialic acid uptake, providing insight into how TRAP transporter function might be inhibited in vivo.
External linksNat Commun / PubMed:35927235 / PubMed Central
MethodsEM (single particle)
Resolution4.7 Å
Structure data

13930

7qe5

EMDB-13930: 3D reconstruction of the membrane domains of the sialic acid TRAP transporter HiSiaQM from Haemophilus influenzae in lipid nanodiscs bound to a high affinity megabody
PDB-7qe5: Structure of the membrane domains of the sialic acid TRAP transporter HiSiaQM from Haemophilus influenzae
Method: EM (single particle) / Resolution: 4.7 Å

Source
  • haemophilus influenzae (bacteria)
  • vicugna pacos (alpaca)
KeywordsTRANSPORT PROTEIN / membrane transporter / TRAP / sialic acid / elevator

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