5yl7
From Proteopedia
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<StructureSection load='5yl7' size='340' side='right' caption='[[5yl7]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='5yl7' size='340' side='right' caption='[[5yl7]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5yl7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Pseudoalteromonas_arctica Pseudoalteromonas arctica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YL7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yl7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_18437 Dsm 18437] and [http://en.wikipedia.org/wiki/Pseudoalteromonas_arctica Pseudoalteromonas arctica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YL7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YL7 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=5yl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yl7 OCA], [http://pdbe.org/5yl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yl7 RCSB], [http://www.ebi.ac.uk/pdbsum/5yl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yl7 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=5yl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yl7 OCA], [http://pdbe.org/5yl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yl7 RCSB], [http://www.ebi.ac.uk/pdbsum/5yl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yl7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzymes isolated from organisms found in cold habitats generally exhibit higher catalytic activity at low temperatures than their mesophilic homologs and are therefore known as cold-active enzymes. Cold-active proteases are very useful in a variety of biotechnological applications, particularly as active ingredients in laundry and dishwashing detergents, where they provide strong protein-degrading activity in cold water. We identified a cold-active protease (Pro21717) from a psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, and determined the crystal structure of its catalytic domain (CD) at a resolution of 1.4 A. The Pro21717-CD structure shows a conserved subtilisin-like fold with a typical catalytic triad (Asp185, His244, and Ser425) and contains four calcium ions and three disulfide bonds. Interestingly, we observed an unexpected electron density at the substrate-binding site from a co-purified peptide. Although the sequence of this peptide is unknown, analysis of the peptide-complexed structure nonetheless provides some indication of the substrate recognition and binding mode of Pro21717. Moreover, various parameters, including a wide substrate pocket size, an abundant active-site loop content, and a flexible structure provide potential explanations for the cold-adapted properties of Pro21717. In conclusion, this is first structural characterization of a cold-adapted subtilisin-like protease, and these findings provide a structural and functional basis for industrial applications of Pro21717 as a cold-active laundry or dishwashing detergent enzyme. | ||
| + | |||
| + | Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 A resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzyme.,Park HJ, Lee CW, Kim D, Do H, Han SJ, Kim JE, Koo BH, Lee JH, Yim JH PLoS One. 2018 Feb 21;13(2):e0191740. doi: 10.1371/journal.pone.0191740., eCollection 2018. PMID:29466378<ref>PMID:29466378</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5yl7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Dsm 18437]] | ||
[[Category: Pseudoalteromonas arctica]] | [[Category: Pseudoalteromonas arctica]] | ||
[[Category: Lee, C W]] | [[Category: Lee, C W]] | ||
Revision as of 07:47, 12 September 2018
Proteases from Pseudoalteromonas arctica PAMC 21717 (Pro21717)
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