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TitleStructure of Perinereis linea erythrocruorin reveals a compact extracellular globin megacomplex.
Journal, issue, pagesStructure, Vol. 34, Issue 8, Page 1123-11133.e3, Year 2026
Publish dateAug 6, 2026
AuthorsJia-Xin Deng / Wen-Bin Cheng / Kang Xu / Pu Hou / Yuxing Chen / Yong-Liang Jiang / Cong-Zhao Zhou /
PubMed AbstractMany invertebrates lack erythrocytes and instead rely on extracellular hemoglobin assemblies, termed erythrocruorins, for oxygen transport. Here we report a 2.84 Å cryo-electron microscopy (cryo-EM) ...Many invertebrates lack erythrocytes and instead rely on extracellular hemoglobin assemblies, termed erythrocruorins, for oxygen transport. Here we report a 2.84 Å cryo-electron microscopy (cryo-EM) structure of Perinereis linea erythrocruorin (PlEc). PlEc is a ∼3.3 MDa megacomplex composed of 180 polypeptide chains organized into 12 protomers, forming a hexagonal bilayer with D6 symmetry. Each protomer consists of 12 globin subunits and three linker subunits, adopting a mushroom-like architecture. The cap of the mushroom is formed by a globin dodecamer associated with a heterotrimeric linker head, and the stem consists of a triple-stranded coiled coil derived from the N-terminal helices of three linker subunits. Biochemical assays show that PlEc has thermal stability and auto-oxidation rate comparable to those of other erythrocruorins, but displays relatively lower oxygen-binding affinity. These findings provide mechanistic insights into the quaternary assembly of invertebrate erythrocruorins and lay the groundwork for the potential biomedical applications.
External linksStructure / PubMed:42398506
MethodsEM (single particle)
Resolution2.84 Å
Structure data

68387

22jw

EMDB-68387, PDB-22jw:
Perinereis linea erythrocruorin
Method: EM (single particle) / Resolution: 2.84 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-CA:
Unknown entry

Source
  • perinereis linea (invertebrata)
KeywordsOXYGEN TRANSPORT / invertebrate / annelid / hemoglobin / erythrocruorin

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