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TitleCryo-EM reveals mechanisms of angiotensin I-converting enzyme allostery and dimerization.
Journal, issue, pagesEMBO J, Vol. 41, Issue 16, Page e110550, Year 2022
Publish dateJul 12, 2022
AuthorsLizelle Lubbe / Bryan Trevor Sewell / Jeremy D Woodward / Edward D Sturrock /
PubMed AbstractHypertension (high blood pressure) is a major risk factor for cardiovascular disease, which is the leading cause of death worldwide. The somatic isoform of angiotensin I-converting enzyme (sACE) ...Hypertension (high blood pressure) is a major risk factor for cardiovascular disease, which is the leading cause of death worldwide. The somatic isoform of angiotensin I-converting enzyme (sACE) plays a critical role in blood pressure regulation, and ACE inhibitors are thus widely used to treat hypertension and cardiovascular disease. Our current understanding of sACE structure, dynamics, function, and inhibition has been limited because truncated, minimally glycosylated forms of sACE are typically used for X-ray crystallography and molecular dynamics simulations. Here, we report the first cryo-EM structures of full-length, glycosylated, soluble sACE (sACE ). Both monomeric and dimeric forms of the highly flexible apo enzyme were reconstructed from a single dataset. The N- and C-terminal domains of monomeric sACE were resolved at 3.7 and 4.1 Å, respectively, while the interacting N-terminal domains responsible for dimer formation were resolved at 3.8 Å. Mechanisms are proposed for intradomain hinging, cooperativity, and homodimerization. Furthermore, the observation that both domains were in the open conformation has implications for the design of sACE modulators.
External linksEMBO J / PubMed:35818993 / PubMed Central
MethodsEM (single particle)
Resolution3.63 - 4.34 Å
Structure data

13797

7q3y

EMDB-13797, PDB-7q3y:
Structure of full-length, monomeric, soluble somatic angiotensin I-converting enzyme showing the N- and C-terminal ellipsoid domains
Method: EM (single particle) / Resolution: 4.34 Å

13799

7q49

EMDB-13799, PDB-7q49:
Local refinement structure of the N-domain of full-length, monomeric, soluble somatic angiotensin I-converting enzyme
Method: EM (single particle) / Resolution: 3.72 Å

13801

7q4c

EMDB-13801, PDB-7q4c:
Local refinement structure of the C-domain of full-length, monomeric, soluble somatic angiotensin I-converting enzyme
Method: EM (single particle) / Resolution: 4.08 Å

EMDB-13802: Structure of full-length, dimeric, soluble somatic angiotensin I-converting enzyme
Method: EM (single particle) / Resolution: 3.79 Å

13803

7q4d

EMDB-13803, PDB-7q4d:
Local refinement structure of the two interacting N-domains of full-length, dimeric, soluble somatic angiotensin I-converting enzyme
Method: EM (single particle) / Resolution: 3.78 Å

13804

7q4e

EMDB-13804, PDB-7q4e:
Local refinement structure of a single N-domain of full-length, dimeric, soluble somatic angiotensin I-converting enzyme
Method: EM (single particle) / Resolution: 3.63 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry / Chloride

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Zinc metalloprotease Dicarboxypeptidase Glycoprotein

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