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Structure paper

TitleIllumination of serotonin transporter mechanism and role of the allosteric site.
Journal, issue, pagesSci Adv, Vol. 7, Issue 49, Page eabl3857, Year 2021
Publish dateDec 3, 2021
AuthorsDongxue Yang / Eric Gouaux /
PubMed AbstractThe serotonin transporter (SERT) terminates serotonin signaling by using sodium and chloride gradients to drive reuptake of serotonin into presynaptic neurons and is the target of widely used ...The serotonin transporter (SERT) terminates serotonin signaling by using sodium and chloride gradients to drive reuptake of serotonin into presynaptic neurons and is the target of widely used medications to treat neuropsychiatric disorders. Despite decades of study, the molecular mechanism of serotonin transport, the coupling to ion gradients, and the role of the allosteric site have remained elusive. Here, we present cryo–electron microscopy structures of SERT in serotonin-bound and serotonin-free states, in the presence of sodium or potassium, resolving all fundamental states of the transport cycle. From the SERT-serotonin complex, we localize the substrate-bound allosteric site, formed by an aromatic pocket positioned in the scaffold domain in the extracellular vestibule, connected to the central site via a short tunnel. Together with elucidation of multiple apo state conformations, we provide previously unseen structural understanding of allosteric modulation, demonstrating how SERT binds serotonin from synaptic volumes and promotes unbinding into the presynaptic neurons.
External linksSci Adv / PubMed:34851672 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.1 Å
Structure data

23361

7li6

EMDB-23361, PDB-7li6:
apo SERT reconstituted in lipid nanodisc in KCl
Method: EM (single particle) / Resolution: 3.5 Å

23362

7li7

EMDB-23362, PDB-7li7:
apo serotonin transporter reconstituted in lipid nanodisc in presence of NaCl in occluded conformation
Method: EM (single particle) / Resolution: 4.1 Å

23363

7li8

EMDB-23363, PDB-7li8:
apo serotonin transporter reconstituted in lipid nanodisc in presence of NaCl in inward open conformation
Method: EM (single particle) / Resolution: 3.9 Å

23364

7li9

EMDB-23364, PDB-7li9:
5-HT bound serotonin transporter reconstituted in lipid nanodisc in KCl
Method: EM (single particle) / Resolution: 3.9 Å

23365

7lia

EMDB-23365, PDB-7lia:
5-HT bound serotonin transporter reconstituted in lipid nanodisc in presence of NaCl in outward facing conformation
Method: EM (single particle) / Resolution: 3.3 Å

23830

7mgw

EMDB-23830, PDB-7mgw:
5-HT bound serotonin transporter reconstituted in lipid nanodisc in NaCl in occluded conformation
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-CL:
Unknown entry / Chloride

ChemComp-R16:
HEXADECANE / Hexadecane

ChemComp-HP6:
HEPTANE / Heptane

ChemComp-D10:
DECANE / Decane

ChemComp-D12:
DODECANE / Dodecane

ChemComp-LNK:
PENTANE / Pentane

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-SRO:
SEROTONIN / neurotransmitter*YM / Serotonin

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
  • Mouse (mice)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / serotonin / human serotonin transporter / transport / Fab / occluded / serotonin transporter / inward / KCl / outward open

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