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TitleStructural basis of purine nucleotide inhibition of human uncoupling protein 1.
Journal, issue, pagesSci Adv, Vol. 9, Issue 22, Page eadh4251, Year 2023
Publish dateJun 2, 2023
AuthorsScott A Jones / Prerana Gogoi / Jonathan J Ruprecht / Martin S King / Yang Lee / Thomas Zögg / Els Pardon / Deepak Chand / Stefan Steimle / Danielle M Copeman / Camila A Cotrim / Jan Steyaert / Paul G Crichton / Vera Moiseenkova-Bell / Edmund R S Kunji /
PubMed AbstractMitochondrial uncoupling protein 1 (UCP1) gives brown adipose tissue of mammals its specialized ability to burn calories as heat for thermoregulation. When activated by fatty acids, UCP1 catalyzes ...Mitochondrial uncoupling protein 1 (UCP1) gives brown adipose tissue of mammals its specialized ability to burn calories as heat for thermoregulation. When activated by fatty acids, UCP1 catalyzes the leak of protons across the mitochondrial inner membrane, short-circuiting the mitochondrion to generate heat, bypassing ATP synthesis. In contrast, purine nucleotides bind and inhibit UCP1, regulating proton leak by a molecular mechanism that is unclear. We present the cryo-electron microscopy structure of the GTP-inhibited state of UCP1, which is consistent with its nonconducting state. The purine nucleotide cross-links the transmembrane helices of UCP1 with an extensive interaction network. Our results provide a structural basis for understanding the specificity and pH dependency of the regulatory mechanism. UCP1 has retained all of the key functional and structural features required for a mitochondrial carrier-like transport mechanism. The analysis shows that inhibitor binding prevents the conformational changes that UCP1 uses to facilitate proton leak.
External linksSci Adv / PubMed:37256948 / PubMed Central
MethodsEM (single particle)
Resolution3.8 Å
Structure data

29857

8g8w

EMDB-29857, PDB-8g8w:
Molecular mechanism of nucleotide inhibition of human uncoupling protein 1
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

Source
  • homo sapiens (human)
  • escherichia coli (strain k12) (bacteria)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / SLC25 / mitochondrial carrier / uncoupling

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