4y42

Cyanase (CynS) from Serratia proteamaculans

spinqualitylabelsall models 4y42, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4y42 is a 10 chain structure with sequence from Serratia proteamaculans 568. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.09Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CYNS_SERP5 Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. Publication Abstract from PubMed 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 A 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. Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans.,Butryn A, Stoehr G, Linke-Winnebeck C, Hopfner KP Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):471-6. doi:, 10.1107/S2053230X15004902. Epub 2015 Mar 21. PMID:25849512 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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