ArticleThe Journal of biological chemistry2014
Structure and mechanism of the phycobiliprotein lyase CpcT.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 36 citations in OpenAlex.
- Improved Stability and Brightness Following Iterative Redesign of a De Novo Biliprotein.Biochemistry · 2026Article
- Dynamic Changes in the Thylakoid Proteome of Cyanobacteria during Light-Regulated Thylakoid Membrane Development.Plants (Basel, Switzerland) · 2023Article
- 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 phycoerythrobilin isomerization activity of MpeV inFrontiers in microbiology · 2022Article
- Structural basis of the protochromic green/red photocycle of the chromatic acclimation sensor RcaE.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Crystal structure of a far-red-sensing cyanobacteriochrome reveals an atypical bilin conformation and spectral tuning mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- CpeF is the bilin lyase that ligates the doubly linked phycoerythrobilin on β-phycoerythrin in the cyanobacteriumThe Journal of biological chemistry · 2019Article
- 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
- Distinct Features of Cyanophage-encoded T-type Phycobiliprotein Lyase ΦCpeT: THE ROLE OF AUXILIARY METABOLIC GENES.The Journal of biological chemistry · 2017Article
- Adaptation to Blue Light in MarineFrontiers in microbiology · 2017Article
- The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- 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
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Authors and funding
9 authors at 2 institutions in 2 countries.
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Abstract
Pigmentation of light-harvesting phycobiliproteins of cyanobacteria requires covalent attachment of open-chain tetrapyrroles, bilins, to the apoproteins. Thioether formation via addition of a cysteine residue to the 3-ethylidene substituent of bilins is mediated by lyases. T-type lyases are responsible for attachment to Cys-155 of phycobiliprotein β-subunits. We present crystal structures of CpcT (All5339) from Nostoc (Anabaena) sp. PCC 7120 and its complex with phycocyanobilin at 1.95 and 2.50 Å resolution, respectively. CpcT forms a dimer and adopts a calyx-shaped β-barrel fold. Although the overall structure of CpcT is largely retained upon chromophore binding, arginine residues at the opening of the binding pocket undergo major rotameric rearrangements anchoring the propionate groups of phycocyanobilin. Based on the structure and mutational analysis, a reaction mechanism is proposed that accounts for chromophore stabilization and regio- and stereospecificity of the addition reaction. At the dimer interface, a loop extending from one subunit partially shields the opening of the phycocyanobilin binding pocket in the other subunit. Deletion of the loop or disruptions of the dimer interface significantly reduce CpcT lyase activity, suggesting functional relevance of the dimer. Dimerization is further enhanced by chromophore binding. The chromophore is largely buried in the dimer, but in the monomer, the 3-ethylidene group is accessible for the apophycobiliprotein, preferentially from the chromophore α-side. Asp-163 and Tyr-65 at the β- and α-face near the E-configured ethylidene group, respectively, support the acid-catalyzed nucleophilic Michael addition of cysteine 155 of the apoprotein to an N-acylimmonium intermediate proposed by Grubmayr and Wagner (Grubmayr, K., and Wagner, U. G. (1988) Monatsh. Chem. 119, 965-983).
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