Structure of the chromoprotein ovorubin from the golden apple snail ( <i>Pomacea canaliculata</i> )

The golden apple snail (Pomacea canaliculata), an invasive gastropod, produces distinctly bright pink egg masses. The astaxanthin-binding ovorubin (P. canaliculata ovorubin [PcOvo]) is a 300-kDa glycoprotein responsible for the egg coloration. Here, we determine the three-dimensional structure of PcOvo using cryo-electron microscopy (cryo-EM). PcOvo is a heterodecameric protein consisting of two copies of each PcOvo1-5 subunit. The subunits have similar repeated ferredoxin-like structures. N-linked glycosylation sites are identified. Solution x-ray scattering data support the overall architecture of the complex. PcOvo3 and PcOvo5 have hydrophobic pockets that likely bind various hydrophobic compounds. The cryo-EM map and binding experiments suggest that PcOvo5 binds astaxanthin, which is responsible for the pink color of the protein. Our structure provides molecular insights into the nature of the gastropod egg coloration and lays a foundation for further investigation of ovorubin biology and evolution.

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Publication Details

Journal
Protein Science
Published
2025-12-23
DOI
https://doi.org/10.1002/pro.70439
Citations
2
Primary Topic
Mollusks and Parasites Studies
Type
article
Field-Weighted Citation Impact
3.34

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article

Structure of the chromoprotein ovorubin from the golden apple snail ( Pomacea canaliculata )

Grzegorz Sabat, Patcharin Wilasluck, Nawaporn Vinayavekhin, Bich Ngoc Tran et al.
2 citations
Protein Science
Mollusks and Parasites Studies
3.34
article

Structure of the chromoprotein ovorubin from the golden apple snail ( Pomacea canaliculata )

Grzegorz Sabat, Patcharin Wilasluck, Nawaporn Vinayavekhin, Bich Ngoc Tran, Yasuteru Shigeta, Wuan‐Geok Saw, Kittikhun Wangkanont, Kowit Hengphasatporn, Orion Shih
article en
2 citations

Abstract

The golden apple snail (Pomacea canaliculata), an invasive gastropod, produces distinctly bright pink egg masses. The astaxanthin-binding ovorubin (P. canaliculata ovorubin [PcOvo]) is a 300-kDa glycoprotein responsible for the egg coloration. Here, we determine the three-dimensional structure of PcOvo using cryo-electron microscopy (cryo-EM). PcOvo is a heterodecameric protein consisting of two copies of each PcOvo1-5 subunit. The subunits have similar repeated ferredoxin-like structures. N-linked glycosylation sites are identified. Solution x-ray scattering data support the overall architecture of the complex. PcOvo3 and PcOvo5 have hydrophobic pockets that likely bind various hydrophobic compounds. The cryo-EM map and binding experiments suggest that PcOvo5 binds astaxanthin, which is responsible for the pink color of the protein. Our structure provides molecular insights into the nature of the gastropod egg coloration and lays a foundation for further investigation of ovorubin biology and evolution.

Protein ScienceVol. 35(1)
University of Wisconsin–Madison (US), University of Tsukuba (JP), Chulalongkorn University (TH), Nanyang Technological University (SG), National Synchrotron Radiation Research Center (TW)
Chulalongkorn University, National Synchrotron Radiation Research Center, Thailand Science Research and Innovation
Life in Land
Openalex Percentile: Top 7%
Mollusks and Parasites Studies
3.34
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