View source for 4wfi


==Crystal structure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-free state==
<StructureSection load='4wfi' size='340' side='right'caption='[[4wfi]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<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='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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/W0TJ64_9PSEU W0TJ64_9PSEU] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wfi" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cutinase 3D structures|Cutinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomonospora viridis]]
[[Category: Kawai F]]
[[Category: Miyakawa T]]
[[Category: Mizushima H]]
[[Category: Oda M]]
[[Category: Ohtsuka J]]
[[Category: Tanokura M]]