ArticleBiochemistry2013
Structural and biochemical characterization of the bilin lyase CpcS from Thermosynechococcus elongatus.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Improved Stability and Brightness Following Iterative Redesign of a De Novo Biliprotein.Biochemistry · 2026Article
- The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions.International journal of molecular sciences · 2023Review
- Crystal structure and molecular mechanism of an E/F type bilin lyase-isomerase.Structure (London, England : 1993) · 2022Article
- The specificity of the bilin lyase CpcS for chromophore attachment to allophycocyanin in the chlorophyll f-containing cyanobacterium Halomicronima hongdechloris.Photosynthesis research · 2022Article
- The phycoerythrobilin isomerization activity of MpeV inFrontiers in microbiology · 2022Article
- Molecular bases of an alternative dual-enzyme system for light color acclimation of marineProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The structural basis of far-red light absorbance by allophycocyanins.Photosynthesis research · 2021Article
- Characterization of cyanobacterial allophycocyanins absorbing far-red light.Photosynthesis research · 2020Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- CpeF is the bilin lyase that ligates the doubly linked phycoerythrobilin on β-phycoerythrin in the cyanobacteriumThe Journal of biological chemistry · 2019Article
- Article
- De novo synthetic biliprotein design, assembly and excitation energy transfer.Journal of the Royal Society, Interface · 2018Article
- Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Adaptation to Blue Light in MarineFrontiers in microbiology · 2017Article
- Structure and mechanism of the phycobiliprotein lyase CpcT.The Journal of biological chemistry · 2014Article
- Insights into the biosynthesis and assembly of cryptophycean phycobiliproteins.The Journal of biological chemistry · 2014Article
- MpeV is a lyase isomerase that ligates a doubly linked phycourobilin on the β-subunit of phycoerythrin I and II in marine Synechococcus.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
21 authors at 7 institutions in 2 countries.
Funding
Abstract
Cyanobacterial phycobiliproteins have evolved to capture light energy over most of the visible spectrum due to their bilin chromophores, which are linear tetrapyrroles that have been covalently attached by enzymes called bilin lyases. We report here the crystal structure of a bilin lyase of the CpcS family from Thermosynechococcus elongatus (TeCpcS-III). TeCpcS-III is a 10-stranded β barrel with two alpha helices and belongs to the lipocalin structural family. TeCpcS-III catalyzes both cognate as well as noncognate bilin attachment to a variety of phycobiliprotein subunits. TeCpcS-III ligates phycocyanobilin, phycoerythrobilin, and phytochromobilin to the alpha and beta subunits of allophycocyanin and to the beta subunit of phycocyanin at the Cys82-equivalent position in all cases. The active form of TeCpcS-III is a dimer, which is consistent with the structure observed in the crystal. With the use of the UnaG protein and its association with bilirubin as a guide, a model for the association between the native substrate, phycocyanobilin, and TeCpcS was produced.
Indexed as
Identifiers
What OpenQuestion holds
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.