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TitleThe structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 7844, Year 2024
Publish dateSep 8, 2024
AuthorsWenguo Li / Junjiang Peng / Deqiang Yao / Bing Rao / Ying Xia / Qian Wang / Shaobai Li / Mi Cao / Yafeng Shen / Peixiang Ma / Rijing Liao / An Qin / Jie Zhao / Yu Cao /
PubMed AbstractCollagen posttranslational processing is crucial for its proper assembly and function. Disruption of collagen processing leads to tissue development and structure disorders like osteogenesis ...Collagen posttranslational processing is crucial for its proper assembly and function. Disruption of collagen processing leads to tissue development and structure disorders like osteogenesis imperfecta (OI). OI-related collagen processing machinery includes prolyl 3-hydroxylase 1 (P3H1), peptidyl-prolyl cis-trans isomerase B (PPIB), and cartilage-associated protein (CRTAP), with their structural organization and mechanism unclear. We determine cryo-EM structures of the P3H1/CRTAP/PPIB complex. The active sites of P3H1 and PPIB form a face-to-face bifunctional reaction center, indicating a coupled modification mechanism. The structure of the P3H1/CRTAP/PPIB/collagen peptide complex reveals multiple binding sites, suggesting a substrate interacting zone. Unexpectedly, a dual-ternary complex is observed, and the balance between ternary and dual-ternary states can be altered by mutations in the P3H1/PPIB active site and the addition of PPIB inhibitors. These findings provide insights into the structural basis of collagen processing by P3H1/CRTAP/PPIB and the molecular pathology of collagen-related disorders.
External linksNat Commun / PubMed:39245686 / PubMed Central
MethodsEM (single particle)
Resolution3.17 - 3.75 Å
Structure data

36762

8k0e

EMDB-36762, PDB-8k0e:
Human collagen prolyl processing enzyme complex, P3H1/CRTAP heterodimer
Method: EM (single particle) / Resolution: 3.65 Å

36763

8k0f

EMDB-36763, PDB-8k0f:
Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, in its apo state
Method: EM (single particle) / Resolution: 3.37 Å

36765

8k0i

EMDB-36765, PDB-8k0i:
Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, in its dual-ternary state
Method: EM (single particle) / Resolution: 3.62 Å

36774

8k0m

EMDB-36774, PDB-8k0m:
Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, bound to 2-oxoglutarate
Method: EM (single particle) / Resolution: 3.17 Å

36787

8k17

EMDB-36787, PDB-8k17:
Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, bound to collagen alpha-1(I) chain
Method: EM (single particle) / Resolution: 3.18 Å

37097

8kc9

EMDB-37097, PDB-8kc9:
Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, bound to cyclosporin A
Method: EM (single particle) / Resolution: 3.75 Å

Chemicals

ChemComp-FE:
Unknown entry

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

ChemComp-AKG:
2-OXOGLUTARIC ACID

Source
  • homo sapiens (human)
  • tolypocladium inflatum (fungus)
KeywordsCYTOSOLIC PROTEIN / complex / hydroxylase / collagen / ER protein

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