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Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans
Author(s) -
Butryn Agata,
Stoehr Gabriele,
LinkeWinnebeck Christian,
Hopfner KarlPeter
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15004902
Subject(s) - cyanate , chemistry , crystallization , active site , ligand (biochemistry) , crystallography , molecule , escherichia coli , stereochemistry , enzyme , biochemistry , organic chemistry , receptor , gene
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 P 1 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.