ArticleiScience2020
Asymmetric Open-Closed Dimer Mechanism of Polyhydroxyalkanoate Synthase PhaC.
Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
The trial behind it
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Who cites it
13 citing papers in PubMed, 42 citations in OpenAlex.
- Biosynthesis of poly(ester amide)s in engineered Escherichia coli.Nature chemical biology · 2025Article
- Structures of Polyhydroxyalkanoate Synthase PhaC from Aeromonas caviae, Producing Biodegradable Plastics.Angewandte Chemie (International ed. in English) · 2025Article
- Enhanced Crystallization of Sustainable Polylactic Acid Composites Incorporating Recycled Industrial Cement.Polymers · 2024Article
- Exogenous Trehalose Improves Growth, Glycogen and Poly-3-Hydroxybutyrate (PHB) Contents in Photoautotrophically GrownBiology · 2024Article
- N-terminal truncation of PhaCMicrobial cell factories · 2024Article
- Article
- Exploring Class I polyhydroxyalkanoate synthases with broad substrate specificity for polymerization of structurally diverse monomer units.Frontiers in bioengineering and biotechnology · 2023Article
- A review on poly(3-hydroxybutyrate-Frontiers in bioengineering and biotechnology · 2022Review
- High natural PHA production from acetate in Cobetia sp. MC34 and Cobetia marina DSM 4741Microbial cell factories · 2021Article
- Tools for the discovery of biopolymer producing cysteine relays.Biophysical reviews · 2021Review
- Engineering ofFrontiers in bioengineering and biotechnology · 2021Article
- Article
- Engineering the YeastFrontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biodegradable polyester polyhydroxyalkanoate (PHA) is a promising bioplastic material for industrial use as a replacement for petroleum-based plastics. PHA synthase PhaC forms an active dimer to polymerize acyl moieties from the substrate acyl-coenzyme A (CoA) into PHA polymers. Here we present the crystal structure of the catalytic domain of PhaC from Chromobacterium sp. USM2, bound to CoA. The structure reveals an asymmetric dimer, in which one protomer adopts an open conformation bound to CoA, whereas the other adopts a closed conformation in a CoA-free form. The open conformation is stabilized by the asymmetric dimerization and enables PhaC to accommodate CoA and also to create the product egress path. The bound CoA molecule has its β-mercaptoethanolamine moiety extended into the active site with the terminal SH group close to active center Cys291, enabling formation of the reaction intermediate by acylation of Cys291.
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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.