4Y42

Cyanase (CynS) from Serratia proteamaculans

Summary for 4Y42

• Entry DOI: 10.2210/pdb4y42/pdb
• Descriptor: Cyanate hydratase, GLYCEROL (3 entities in total)
• Functional Keywords: cyns, cyanase, lyase
• Biological source: Serratia proteamaculans
• Total number of polymer chains: 10
• Total formula weight: 172096.21

Authors

Butryn, A.,Hopfner, K.-P. (deposition date: 2015-02-10, release date: 2015-04-08, Last modification date: 2024-01-10)

Primary citation

Butryn, A.,Stoehr, G.,Linke-Winnebeck, C.,Hopfner, K.-P.
Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans
Acta Crystallogr.,Sect.F, 71:471-476, 2015

PubMed 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.

PubMed: 25849512
DOI: 10.1107/S2053230X15004902

Experimental method

X-RAY DIFFRACTION (2.09 Å)