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| | <StructureSection load='4y42' size='340' side='right'caption='[[4y42]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='4y42' size='340' side='right'caption='[[4y42]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y42]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Serratia_proteamaculans Serratia proteamaculans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y42 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y42 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y42]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_proteamaculans_568 Serratia proteamaculans 568]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y42 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyanase Cyanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.104 4.2.1.104] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4y42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y42 OCA], [https://pdbe.org/4y42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y42 RCSB], [https://www.ebi.ac.uk/pdbsum/4y42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y42 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y42 OCA], [http://pdbe.org/4y42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y42 RCSB], [http://www.ebi.ac.uk/pdbsum/4y42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y42 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYNS_SERP5 CYNS_SERP5]] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. | + | [https://www.uniprot.org/uniprot/CYNS_SERP5 CYNS_SERP5] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cyanase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Serratia proteamaculans]] | + | [[Category: Serratia proteamaculans 568]] |
| - | [[Category: Butryn, A]] | + | [[Category: Butryn A]] |
| - | [[Category: Hopfner, K P]] | + | [[Category: Hopfner K-P]] |
| - | [[Category: Cyn]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Butryn A, Stoehr G, Linke-Winnebeck C, Hopfner KP. Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans. Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):471-6. doi:, 10.1107/S2053230X15004902. Epub 2015 Mar 21. PMID:25849512 doi:http://dx.doi.org/10.1107/S2053230X15004902
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