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TitleDimerization and dynamics of human angiotensin-I converting enzyme revealed by cryo-EM and MD simulations.
Journal, issue, pagesElife, Vol. 14, Year 2025
Publish dateSep 24, 2025
AuthorsJordan M Mancl / Xiaoyang Wu / Minglei Zhao / Wei-Jen Tang /
PubMed AbstractAngiotensin-I converting enzyme (ACE) regulates the levels of disparate bioactive peptides, notably converting angiotensin-I to angiotensin-II and degrading amyloid beta. ACE is a heavily ...Angiotensin-I converting enzyme (ACE) regulates the levels of disparate bioactive peptides, notably converting angiotensin-I to angiotensin-II and degrading amyloid beta. ACE is a heavily glycosylated dimer, containing four analogous catalytic sites, and exists in membrane-bound and soluble (sACE) forms. ACE inhibition is a frontline, FDA-approved, therapy for cardiovascular diseases yet is associated with significant side effects, including higher rates of lung cancer. To date, structural studies have been confined to individual domains or partially denatured cryo-EM structures. Here, we report the cryo-EM structure of the glycosylated full human sACE dimer. We resolved four structural states at 2.99 - 3.65 Å resolution which are primarily differentiated by varying degrees of solvent accessibility to the active sites and reveal the full dimerization interface. We also employed all-atom molecular dynamics (MD) simulations and heterogeneity analysis in cryoSPARC, cryoDRGN, and RECOVAR to elucidate the conformational dynamics of sACE and identify key regions mediating conformational change. We identify differences in the mechanisms governing the conformational dynamics of individual domains that have implications for the design of domain-specific sACE modulators.
External linksElife / PubMed:40988601 / PubMed Central
MethodsEM (single particle)
Resolution2.99 - 3.65 Å
Structure data

45733

9clx

EMDB-45733, PDB-9clx:
Angiotensin I converting enzyme full-length dimer
Method: EM (single particle) / Resolution: 3.65 Å

46574

9d55

EMDB-46574, PDB-9d55:
Apo ACE full dimer 2 prepared by chameleon
Method: EM (single particle) / Resolution: 3.15 Å

46579

9d5m

EMDB-46579, PDB-9d5m:
Apo ACE full dimer 1 prepared by chameleon
Method: EM (single particle) / Resolution: 3.05 Å

46581

9d5s

EMDB-46581, PDB-9d5s:
Apo ACE full dimer 3 prepared by chameleon
Method: EM (single particle) / Resolution: 2.99 Å

Chemicals

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

Source
  • homo sapiens (human)
KeywordsHYDROLASE / protease / dimer / homodimer / zinc metalloprotease

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