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Structure paper

TitleStructure and function of the SIT1 proline transporter in complex with the COVID-19 receptor ACE2.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 5503, Year 2024
Publish dateJun 29, 2024
AuthorsHuanyu Z Li / Ashley C W Pike / Irina Lotsaris / Gamma Chi / Jesper S Hansen / Sarah C Lee / Karin E J Rödström / Simon R Bushell / David Speedman / Adam Evans / Dong Wang / Didi He / Leela Shrestha / Chady Nasrallah / Nicola A Burgess-Brown / Robert J Vandenberg / Timothy R Dafforn / Elisabeth P Carpenter / David B Sauer /
PubMed AbstractProline is widely known as the only proteogenic amino acid with a secondary amine. In addition to its crucial role in protein structure, the secondary amino acid modulates neurotransmission and ...Proline is widely known as the only proteogenic amino acid with a secondary amine. In addition to its crucial role in protein structure, the secondary amino acid modulates neurotransmission and regulates the kinetics of signaling proteins. To understand the structural basis of proline import, we solved the structure of the proline transporter SIT1 in complex with the COVID-19 viral receptor ACE2 by cryo-electron microscopy. The structure of pipecolate-bound SIT1 reveals the specific sequence requirements for proline transport in the SLC6 family and how this protein excludes amino acids with extended side chains. By comparing apo and substrate-bound SIT1 states, we also identify the structural changes that link substrate release and opening of the cytoplasmic gate and provide an explanation for how a missense mutation in the transporter causes iminoglycinuria.
External linksNat Commun / PubMed:38951531 / PubMed Central
MethodsEM (single particle)
Resolution3.24 - 3.76 Å
Structure data

17377

8p2w

EMDB-17377, PDB-8p2w:
Structure of human SIT1 (focussed map / refinement)
Method: EM (single particle) / Resolution: 3.76 Å

17378

8p2x

EMDB-17378, PDB-8p2x:
Structure of human SIT1:ACE2 complex (open PD conformation)
Method: EM (single particle) / Resolution: 3.59 Å

17379

8p2y

EMDB-17379, PDB-8p2y:
Structure of human SIT1:ACE2 complex (closed PD conformation)
Method: EM (single particle) / Resolution: 3.46 Å

17380

8p2z

EMDB-17380, PDB-8p2z:
Structure of human SIT1 bound to L-pipecolate (focussed map / refinement)
Method: EM (single particle) / Resolution: 3.5 Å

17381

8p30

EMDB-17381, PDB-8p30:
Structure of human SIT1:ACE2 complex (open PD conformation) bound to L-pipecolate
Method: EM (single particle) / Resolution: 3.29 Å

17382

8p31

EMDB-17382, PDB-8p31:
Structure of human SIT1:ACE2 complex (closed PD conformation) bound to L-pipecolate
Method: EM (single particle) / Resolution: 3.24 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

ChemComp-NDG:
2-acetamido-2-deoxy-alpha-D-glucopyranose

ChemComp-YCP:
(2S)-piperidine-2-carboxylic acid

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / COVID-19 receptor / amino acid transport / amino acid transporter / proline / SLC6A20 / ACE2

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