ArticleStructure (London, England : 1993)2009
Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 66 citations in OpenAlex.
- Coupled Binuclear Copper Sites in Biology: An Experimentally-Calibrated Computational Perspective.Coordination chemistry reviews · 2025Article
- Article
- Similar but Still Different: Which Amino Acid Residues Are Responsible for Varying Activities in Type-III Copper Enzymes?Chembiochem : a European journal of chemical biology · 2021Review
- Myriapod haemocyanin: the first three-dimensional reconstruction ofOpen biology · 2020Article
- Hemocyanin facilitates lignocellulose digestion by wood-boring marine crustaceans.Nature communications · 2018Article
- Diversity, evolution, and function of myriapod hemocyanins.BMC evolutionary biology · 2018Article
- Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidases.Scientific reports · 2017Article
- Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin.Cellular and molecular life sciences : CMLS · 2017Review
- The structure of a prophenoloxidase (PPO) from Anopheles gambiae provides new insights into the mechanism of PPO activation.BMC biology · 2016Article
- Structure and Characterization of Eriphia verrucosa Hemocyanin.Marine biotechnology (New York, N.Y.) · 2015Article
- Mechanistic studies of the tyrosinase-catalyzed oxidative cyclocondensation of 2-aminophenol to 2-aminophenoxazin-3-one.Archives of biochemistry and biophysics · 2015Article
- Copper active sites in biology.Chemical reviews · 2014Review
- Article
- Origin, evolution and classification of type-3 copper proteins: lineage-specific gene expansions and losses across the Metazoa.BMC evolutionary biology · 2013Article
- Cryo-EM structure of a molluscan hemocyanin suggests its allosteric mechanism.Structure (London, England : 1993) · 2013Article
- Cryo-electron microscopy--a primer for the non-microscopist.The FEBS journal · 2013Review
- Site-directed mutagenesis of a tetrameric dandelion polyphenol oxidase (PPO-6) reveals the site of subunit interaction.Plant molecular biology · 2012Article
- Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.The EMBO journal · 2012Article
- Crystallization and preliminary analysis of crystals of the 24-meric hemocyanin of the emperor scorpion (Pandinus imperator).PloS one · 2012Article
- Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus.Nature structural & molecular biology · 2010Article
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Authors and funding
9 authors at 2 institutions in 3 countries.
Funding
Abstract
Phenoloxidases (POs) occur in all organisms and are involved in skin and hair coloring in mammals, and initiating melanization in wound healing. Mutation or overexpression of PO can cause albinism or melanoma, respectively. SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in each subunit, exposing the entrance to the active site; this movement is stabilized by enhanced interhexamer and interdodecamer interactions, particularly in the central linker subunits. This mechanism could be applicable to other type 3 copper proteins, as the active site is highly conserved.
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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.