4wfi
From Proteopedia
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| - | ''' | + | ==Crystal strucrure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-free state== |
| + | <StructureSection load='4wfi' size='340' side='right' caption='[[4wfi]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wfi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WFI FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wfj|4wfj]], [[4wfk|4wfk]]</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=4wfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wfi RCSB], [http://www.ebi.ac.uk/pdbsum/4wfi PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A cutinase-like enzyme from Saccharomonospora viridis AHK190, Cut190, hydrolyzes the inner block of polyethylene terephthalate (PET); this enzyme is a member of the lipase family, which contains an alpha/beta hydrolase fold and a Ser-His-Asp catalytic triad. The thermostability and activity of Cut190 are enhanced by high concentrations of calcium ions, which is essential for the efficient enzymatic hydrolysis of amorphous PET. Although Ca2+-induced thermostabilization and activation of enzymes have been well explored in alpha-amylases, the mechanism for PET-degrading cutinase-like enzymes remains poorly understood. We focused on the mechanisms by which Ca2+ enhances these properties, and we determined the crystal structures of a Cut190 S226P mutant (Cut190S226P) in the Ca2+-bound and free states at 1.75 and 1.45 A resolution, respectively. Based on the crystallographic data, a Ca2+ ion was coordinated by four residues within loop regions (the Ca2+ site) and two water molecules in a tetragonal bipyramidal array. Furthermore, the binding of Ca2+ to Cut190S226P induced large conformational changes in three loops, which were accompanied by the formation of additional interactions. The binding of Ca2+ not only stabilized a region that is flexible in the Ca2+-free state but also modified the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily. Thus, our study explains the structural basis of Ca2+-enhanced thermostability and activity in PET-degrading cutinase-like enzyme for the first time and found that the inactive state of Cut190S226P is activated by a conformational change in the active-site sealing residue, F106. | ||
| - | + | Structural basis for the Ca-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190.,Miyakawa T, Mizushima H, Ohtsuka J, Oda M, Kawai F, Tanokura M Appl Microbiol Biotechnol. 2014 Dec 11. PMID:25492421<ref>PMID:25492421</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kawai, F]] | ||
| + | [[Category: Miyakawa, T]] | ||
| + | [[Category: Mizushima, H]] | ||
| + | [[Category: Oda, M]] | ||
| + | [[Category: Ohtsuka, J]] | ||
| + | [[Category: Tanokura, M]] | ||
| + | [[Category: Alpha/beta-hydrolase fold]] | ||
| + | [[Category: Cutinase]] | ||
| + | [[Category: Polyesterase]] | ||
Revision as of 10:48, 24 December 2014
Crystal strucrure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-free state
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