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4wfk

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Revision as of 01:57, 10 March 2017

Crystal structure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-bound state at 2.35 angstrom resolution

Structural highlights

4wfk is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4wfi, 4wfj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 Publication Abstract from PubMed
3 See Also
4 References

Proteopedia Page Contributors and Editors (what is this?)

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-bound state at 2.35 angstrom resolution==
 <StructureSection load='4wfk' size='340' side='right' caption='[[4wfk]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wfi|4wfi]], [[4wfj|4wfj]]</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=4wfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wfk RCSB], [http://www.ebi.ac.uk/pdbsum/4wfk PDBsum]</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=4wfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfk OCA], [http://pdbe.org/4wfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wfk RCSB], [http://www.ebi.ac.uk/pdbsum/4wfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wfk ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4wfk" style="background-color:#fffaf0;"></div>
 ==See Also==

4wfk

From Proteopedia

Revision as of 01:57, 10 March 2017

Crystal structure of PET-degrading cutinase Cut190 S226P mutant in Ca(2+)-bound state at 2.35 angstrom resolution

Structural highlights

Publication Abstract from PubMed

See Also

References

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