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4wfi

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Crystal structure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-free state

Structural highlights

4wfi is a 1 chain structure with sequence from Saccharomonospora viridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wfi"

@@ Line 1: / Line 1: @@
-==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]] 1.45&Aring;' scene=''>
+==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. 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='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>
+== Function ==
+[https://www.uniprot.org/uniprot/W0TJ64_9PSEU W0TJ64_9PSEU]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 16: @@
 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: Kawai, F]]
+[[Category: Large Structures]]
-[[Category: Miyakawa, T]]
+[[Category: Saccharomonospora viridis]]
-[[Category: Mizushima, H]]
+[[Category: Kawai F]]
-[[Category: Oda, M]]
+[[Category: Miyakawa T]]
-[[Category: Ohtsuka, J]]
+[[Category: Mizushima H]]
-[[Category: Tanokura, M]]
+[[Category: Oda M]]
-[[Category: Alpha/beta-hydrolase fold]]
+[[Category: Ohtsuka J]]
-[[Category: Cutinase]]
+[[Category: Tanokura M]]
-[[Category: Polyesterase]]

4wfi

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Current revision

Crystal structure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-free state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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