Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans. Issue 4 (1st April 2015)

• Record Type: Journal Article
• Authors: Butryn, Agata; Stoehr, Gabriele; Linke‐Winnebeck, Christian; Hopfner, Karl‐Peter
• Is Part Of: Acta crystallographica. Volume 71:Issue 4(2015:Apr.)
• Page Start: 471
• Page End: 476
• Publication Date: 2015-04-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15004902
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Cyanate hydratase (CynS) catalyzes the decomposition of cyanate and bicarbonate into ammonia and carbon dioxide. Here, the serendipitous crystallization of CynS from <italic>Serratia proteamaculans</italic> (SpCynS) is reported. SpCynS was crystallized as an impurity and its identity was determined using mass‐spectrometric analysis. The crystals belonged to space group <italic>P</italic>1 and diffracted to 2.1 Å resolution. The overall structure of SpCynS is very similar to a previously determined structure of CynS from <italic>Escherichia coli</italic>. 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.</p> </abstract>