ArticleActa crystallographica. Section F, Structural biology communications2015
Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Structural mechanism of Escherichia coli cyanase.Acta crystallographica. Section D, Structural biology · 2023Article
- Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation.Scientific reports · 2021Article
- Detecting the nature and solving the crystal structure of a contaminant protein from an opportunistic pathogen.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Cyanate Assimilation by the Alkaliphilic Cyanide-Degrading BacteriumInternational journal of molecular sciences · 2019Article
- Expression of the cyanobacterial enzyme cyanase increases cyanate metabolism and cyanate tolerance in Arabidopsis.Environmental science and pollution research international · 2017Article
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Abstract
Cyanate hydratase (CynS) catalyzes the decomposition of cyanate and bicarbonate into ammonia and carbon dioxide. Here, the serendipitous crystallization of CynS from Serratia proteamaculans (SpCynS) is reported. SpCynS was crystallized as an impurity and its identity was determined using mass-spectrometric analysis. The crystals belonged to space group P1 and diffracted to 2.1 Å resolution. The overall structure of SpCynS is very similar to a previously determined structure of CynS from Escherichia coli. Density for a ligand bound to the SpCynS active site was observed, but could not be unambiguously identified. Additionally, glycerol molecules bound at the entry to the active site of the enzyme indicate conserved residues that might be important for the trafficking of substrates and products.
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