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| | <StructureSection load='4wfi' size='340' side='right'caption='[[4wfi]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='4wfi' size='340' side='right'caption='[[4wfi]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wfi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"saccharomonospora_internatus"_(agre_et_al._1974)_greiner-mai_et_al._1988 "saccharomonospora internatus" (agre et al. 1974) greiner-mai et al. 1988]. 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> | + | <table><tr><td colspan='2'>[[4wfi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomonospora_viridis Saccharomonospora viridis]. 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 [https://proteopedia.org/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> | + | </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=4wfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfi OCA], [https://pdbe.org/4wfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wfi RCSB], [https://www.ebi.ac.uk/pdbsum/4wfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wfi ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cut190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1852 "Saccharomonospora internatus" (Agre et al. 1974) Greiner-Mai et al. 1988])</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://pdbe.org/4wfi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wfi RCSB], [http://www.ebi.ac.uk/pdbsum/4wfi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wfi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/W0TJ64_9PSEU W0TJ64_9PSEU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kawai, F]] | + | [[Category: Saccharomonospora viridis]] |
| - | [[Category: Miyakawa, T]] | + | [[Category: Kawai F]] |
| - | [[Category: Mizushima, H]] | + | [[Category: Miyakawa T]] |
| - | [[Category: Oda, M]] | + | [[Category: Mizushima H]] |
| - | [[Category: Ohtsuka, J]] | + | [[Category: Oda M]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Ohtsuka J]] |
| - | [[Category: Alpha/beta-hydrolase fold]]
| + | [[Category: Tanokura M]] |
| - | [[Category: Cutinase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Polyesterase]]
| + | |
| Structural highlights
Function
W0TJ64_9PSEU
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miyakawa T, Mizushima H, Ohtsuka J, Oda M, Kawai F, Tanokura M. Structural basis for the Ca-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190. Appl Microbiol Biotechnol. 2014 Dec 11. PMID:25492421 doi:http://dx.doi.org/10.1007/s00253-014-6272-8
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