ArticleStructure (London, England : 1993)2013
Cryo-EM structure of a molluscan hemocyanin suggests its allosteric mechanism.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Increased functional unit flexibility and solvent accessibility favours oxygen capture in molluscan hemocyanin.RSC advances · 2025Article
- Classification of polyphenol oxidases shows ancient gene duplication leading to two distinct enzyme types.iScience · 2025Article
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- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Hemocyanin of the caenogastropod Pomacea canaliculata exhibits evolutionary differences among gastropod clades.PloS one · 2020Article
- Article
- Protein-Metal-Ion Interactions Studied by Mass Spectrometry-Based Footprinting with Isotope-Encoded Benzhydrazide.Analytical chemistry · 2019Article
- Proteomics Studies on the three Larval Stages of Development and Metamorphosis of Babylonia areolata.Scientific reports · 2018Article
- Molluscan hemocyanin: structure, evolution, and physiology.Biophysical reviews · 2018Review
- Biological cryo-electron microscopy in China.Protein science : a publication of the Protein Society · 2017Review
- Structural analysis and insertion study reveal the ideal sites for surface displaying foreign peptides on a betanodavirus-like particle.Veterinary research · 2016Article
- Molecular architecture of the Ub-PCNA/Pol η complex bound to DNA.Scientific reports · 2015Article
- On the Ultrastructure and Function of Rhogocytes from the Pond Snail Lymnaea stagnalis.PloS one · 2015Article
- Protruding knob-like proteins violate local symmetries in an icosahedral marine virus.Nature communications · 2014Article
- Article
- Article
- High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy.Ultramicroscopy · 2013Article
- Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice.Microscopy (Oxford, England) · 2013Review
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Authors and funding
10 authors.
Funding
Abstract
Hemocyanins are responsible for transporting O2 in the arthropod and molluscan hemolymph. Haliotis diversicolor molluscan hemocyanin isoform 1 (HdH1) is an 8 MDa oligomer. Each subunit is made up of eight functional units (FUs). Each FU contains two Cu ions, which can reversibly bind an oxygen molecule. Here, we report a 4.5 A° cryo-EM structure of HdH1. The structure clearly shows ten asymmetric units arranged with D5 symmetry. Each asymmetric unit contains two structurally distinct but chemically identical subunits. The map is sufficiently resolved to trace the entire subunit Ca backbone and to visualize densities corresponding to some large side chains, Cu ion pairs, and interaction networks of adjacent subunits. A FU topology path intertwining between the two subunits of the asymmetric unit is unambiguously determined. Our observations suggest a structural mechanism for the stability of the entire hemocyanin didecamer and 20 ‘‘communication clusters’’ across asymmetric units responsible for its allosteric property upon oxygen binding.
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