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TitleCryo-electron microscopy structure and potential enzymatic function of human six-transmembrane epithelial antigen of the prostate 1 (STEAP1).
Journal, issue, pagesJ Biol Chem, Vol. 295, Issue 28, Page 9502-9512, Year 2020
Publish dateJul 10, 2020
AuthorsWout Oosterheert / Piet Gros /
PubMed AbstractSix-transmembrane epithelial antigen of the prostate 1 (STEAP1) is an integral membrane protein that is highly up-regulated on the cell surface of several human cancers, making it a promising ...Six-transmembrane epithelial antigen of the prostate 1 (STEAP1) is an integral membrane protein that is highly up-regulated on the cell surface of several human cancers, making it a promising therapeutic target to manage these diseases. It shares sequence homology with three enzymes (STEAP2-STEAP4) that catalyze the NADPH-dependent reduction of iron(III). However, STEAP1 lacks an intracellular NADPH-binding domain and does not exhibit cellular ferric reductase activity. Thus, both the molecular function of STEAP1 and its role in cancer progression remain elusive. Here, we present a ∼3.0-Å cryo-EM structure of trimeric human STEAP1 bound to three antigen-binding fragments (Fabs) of the clinically used antibody mAb120.545. The structure revealed that STEAP1 adopts a reductase-like conformation and interacts with the Fabs through its extracellular helices. Enzymatic assays in human cells revealed that STEAP1 promotes iron(III) reduction when fused to the intracellular NADPH-binding domain of its family member STEAP4, suggesting that STEAP1 functions as a ferric reductase in STEAP heterotrimers. Our work provides a foundation for deciphering the molecular mechanisms of STEAP1 and may be useful in the design of new therapeutic strategies to target STEAP1 in cancer.
External linksJ Biol Chem / PubMed:32409586 / PubMed Central
MethodsEM (single particle)
Resolution2.97 Å
Structure data

10735

6y9b

EMDB-10735, PDB-6y9b:
Cryo-EM structure of trimeric human STEAP1 bound to three Fab120.545 fragments
Method: EM (single particle) / Resolution: 2.97 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-XP4:
1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHATE / DMPA, phospholipid*YM

Source
  • homo sapiens (human)
  • house mouse (house mouse)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / Integral membrane protein Heme-binding protein Oxidoreductase Antibody-antigen complex

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