ArticleStructure (London, England : 1993)2015
Structure of mega-hemocyanin reveals protein origami in snails.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 33 citations in OpenAlex.
- Programmable Protein-DNA Composite Nanostructures: from Nanostructure Construction to Protein-Induced Micro-Scale Material Self-Assembly and Functionalization.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Article
- The Evolution of Hemocyanin Genes in Caenogastropoda: Gene Duplications and Intron Accumulation in Highly Diverse Gastropods.Journal of molecular evolution · 2021Article
- Hemocyanins of Muricidae: New 'Insights' Unravel an Additional Highly Hydrophilic 800 kDa Mass Within the Molecule.Journal of molecular evolution · 2021Article
- Hemocyanin of the caenogastropod Pomacea canaliculata exhibits evolutionary differences among gastropod clades.PloS one · 2020Article
- Article
- Article
- Molluscan hemocyanin: structure, evolution, and physiology.Biophysical reviews · 2018Review
- Molluskan Hemocyanins Activate the Classical Pathway of the Human Complement System through Natural Antibodies.Frontiers in immunology · 2017Article
- Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin.Cellular and molecular life sciences : CMLS · 2017Review
- On the Ultrastructure and Function of Rhogocytes from the Pond Snail Lymnaea stagnalis.PloS one · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mega-hemocyanin is a 13.5 MDa oxygen transporter found in the hemolymph of some snails. Similar to typical gastropod hemocyanins, it is composed of 400 kDa building blocks but has additional 550 kDa subunits. Together, they form a large, completely filled cylinder. The structural basis for this highly complex protein packing is not known so far. Here, we report the electron cryomicroscopy (cryo-EM) structure of mega-hemocyanin complexes from two different snail species. The structures reveal that mega-hemocyanin is composed of flexible building blocks that differ in their conformation, but not in their primary structure. Like a protein origami, these flexible blocks are optimally packed, implementing different local symmetries and pseudosymmetries. A comparison between the two structures suggests a surprisingly simple evolutionary mechanism leading to these large oxygen transporters.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.