Structure of a secreted lancelet carotenoid cleavage dioxygenase (CCD), from an ancestral CCD clade

Abstract

Carotenoid cleavage dioxygenases (CCDs) are a superfamily of non-heme iron-containing enzymes ubiquitous across all kingdoms of life. Previously, we identified a new subfamily of CCDs termed beta-carotene oxygenase-like (BCOL) proteins, a chordate expansion of an ancestral sister clade of metazoan CCDs, which are widely distributed in marine invertebrates, including mollusks and lancelets. Here we present the three-dimensional structure of a representative BCOL protein from the lancelet Branchiostoma fforidae (BCOLg) at 2.4 Å resolution and its functional properties. BCOLg symmetrically cleaves β-carotene into all- trans retinal. RNAseq of wild-caught animals detected six of the seven annotated BCOL transcripts in Branchiostoma gut tissue. We expressed and crystallized recombinant BCOLg. BCOLg is heavily glycosylated, with four N-linked glycosylation sites, and adopts the seven-bladed propeller fold characteristic of the superfamily, with one disulfide bond contributing to structural stability. BCOLg and several other BCOL proteins contain Asp substitutions at two of three Glu positions found in other CCDs, stabilizing three of four His residues involved in Fe 2+ coordination. Notably, BCOLg lacks the canonical -PDPCK-motif characteristic of other metazoan CCDs.

Summary: Reporting the structure of lancelet beta-carotene oxygenase-like BCOLg protein at 2.4 Å, an unusual carotenoid cleavage dioxygenase (CCD) superfamily member. BCOLg is a heavily glycosylated protein with a distinctive iron-coordination environment and lacking the canonical metazoan -PDPCK-motif.

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BibTeX RIS

BibTeX

@misc{uppal2026structure,
  title = {{Structure of a secreted lancelet carotenoid cleavage dioxygenase (CCD), from an ancestral CCD clade}},
  author = {Sheetal Uppal and Gleysin Cabrera Herrera and Liya Muslinkina and Gowthaman Govindarajan and Yan Li and David N. Garboczi and Igor B. Rogozin and Eugenia Poliakov and Apostolos G. Gittis and T. Michael Redmond},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.29.762971},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.29.762971v1},
  note = {CC BY},
}

RIS

TY  - UNPB
TI  - Structure of a secreted lancelet carotenoid cleavage dioxygenase (CCD), from an ancestral CCD clade
AU  - Sheetal Uppal
AU  - Gleysin Cabrera Herrera
AU  - Liya Muslinkina
AU  - Gowthaman Govindarajan
AU  - Yan Li
AU  - David N. Garboczi
AU  - Igor B. Rogozin
AU  - Eugenia Poliakov
AU  - Apostolos G. Gittis
AU  - T. Michael Redmond
PY  - 2026
DA  - 2026/10/29
PB  - bioRxiv
DO  - 10.64898/2026.10.29.762971
UR  - https://www.biorxiv.org/content/10.64898/2026.10.29.762971v1
AB  - Carotenoid cleavage dioxygenases (CCDs) are a superfamily of non-heme iron-containing enzymes ubiquitous across all kingdoms of life. Previously, we identified a new subfamily of CCDs termed beta-carotene oxygenase-like (BCOL) proteins, a chordate expansion of an ancestral sister clade of metazoan CCDs, which are widely distributed in marine invertebrates, including mollusks and lancelets. Here we present the three-dimensional structure of a representative BCOL protein from the lancelet Branchiostoma fforidae (BCOLg) at 2.4 Å resolution and its functional properties. BCOLg symmetrically cleaves β-carotene into all- trans retinal. RNAseq of wild-caught animals detected six of the seven annotated BCOL transcripts in Branchiostoma gut tissue. We expressed and crystallized recombinant BCOLg. BCOLg is heavily glycosylated, with four N-linked glycosylation sites, and adopts the seven-bladed propeller fold characteristic of the superfamily, with one disulfide bond contributing to structural stability. BCOLg and several other BCOL proteins contain Asp substitutions at two of three Glu positions found in other CCDs, stabilizing three of four His residues involved in Fe 2+ coordination. Notably, BCOLg lacks the canonical -PDPCK-motif characteristic of other metazoan CCDs.  Summary: Reporting the structure of lancelet beta-carotene oxygenase-like BCOLg protein at 2.4 Å, an unusual carotenoid cleavage dioxygenase (CCD) superfamily member. BCOLg is a heavily glycosylated protein with a distinctive iron-coordination environment and lacking the canonical metazoan -PDPCK-motif.
SN  - 2692-8205
ER  -

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