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TitleCryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 4337, Year 2018
Publish dateOct 18, 2018
AuthorsWout Oosterheert / Laura S van Bezouwen / Remco N P Rodenburg / Joke Granneman / Friedrich Förster / Andrea Mattevi / Piet Gros /
PubMed AbstractEnzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe and Cu ions to facilitate metal-ion uptake by mammalian cells. STEAPs are highly upregulated in several ...Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe and Cu ions to facilitate metal-ion uptake by mammalian cells. STEAPs are highly upregulated in several types of cancer, making them potential therapeutic targets. However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive. Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe-NTA. Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer. Substrate binding within a positively charged ring indicates that iron gets reduced while in complex with its chelator. These molecular principles of iron reduction provide a basis for exploring STEAPs as therapeutic targets.
External linksNat Commun / PubMed:30337524 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.8 Å
Structure data

0199

6hcy

EMDB-0199, PDB-6hcy:
human STEAP4 bound to NADP, FAD, heme and Fe(III)-NTA.
Method: EM (single particle) / Resolution: 3.1 Å

0200

6hd1

EMDB-0200, PDB-6hd1:
human STEAP4 bound to NADPH, FAD and heme.
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

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

ChemComp-44E:
(2R)-3-(phosphonooxy)propane-1,2-diyl dihexanoate / phospholipid*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Enzyme / Metalloreductase / Electron Transfer / Cofactor-binding

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