Cutinase
From Proteopedia
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<StructureSection load='4oyl' size='350' side='right' caption='Structure of cutinase (PDB entry [[4oyl]])' scene='55/551226/Cv/1'> | <StructureSection load='4oyl' size='350' side='right' caption='Structure of cutinase (PDB entry [[4oyl]])' scene='55/551226/Cv/1'> | ||
| - | '''Cutinase''' (CUT) | + | '''Cutinase''' (CUT) or '''α/β hydrolase family protein''' the conversion of cutin to cutin monomers. Cutin is a main component of the plant cuticle. Polymeric cutin which is composed of hydroxyl and hydroxyepoxy fatty acids is found in the outer layer of plants. CUT is found in fungi and bacteria. CUT degrades the cutin enabling pathogens’ penetration into plant cells. CUT is inhibited by organophosphates like E600 (diethyl-p-nitrophenyl phosphate) and organophosphonates.<ref>PMID:9175860</ref> |
== Relevance == | == Relevance == | ||
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Upon CUT inhibition by organophosphates the <scene name='55/551226/Cv/3'>catalytic triad of Ser-His-Asp exhibits esterification of Ser and ethylation of His</scene>.<ref>PMID:24832484</ref> | Upon CUT inhibition by organophosphates the <scene name='55/551226/Cv/3'>catalytic triad of Ser-His-Asp exhibits esterification of Ser and ethylation of His</scene>.<ref>PMID:24832484</ref> | ||
| - | </StructureSection> | ||
== 3D Structures of cutinase == | == 3D Structures of cutinase == | ||
| + | [[Cutinase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | **[[1xzl]] – NhCUT + hexylphosphonate ethyl ester<BR /> | ||
| - | **[[1xzk]] – NhCUT + di-isopropyl phosphate <BR /> | ||
| - | **[[1xzm]] – NhCUT + undecyl chloro phosphonate ester<BR /> | ||
| - | **[[3dd5]] – GcCUT + E600 <BR /> | ||
| - | **[[3dea]] – GcCUT + PETFP <BR /> | ||
| - | **[[3ef3]], [[3esa]], [[3esb]], [[3eac]], [[3esd]] – NhCUT + Pt inhibitor <BR /> | ||
| - | **[[3qpc]] – NhCUT + paraoxon <BR /> | ||
| - | **[[3qpd]] – NhCUT + phosphoserine <BR /> | ||
| - | **[[4oyl]] – HiCUT + ethyl phosphate <BR /> | ||
| - | **[[4pse]] – TrCUT + phosphonate derivative<BR /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category: Topic Page]] | [[Category: Topic Page]] | ||
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References
- ↑ Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C. Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. J Mol Biol. 1997 May 16;268(4):779-99. PMID:9175860 doi:http://dx.doi.org/10.1006/jmbi.1997.1000
- ↑ Maiti IB, Kolattukudy PE. Prevention of fungal infection of plants by specific inhibition of cutinase. Science. 1979 Aug 3;205(4405):507-8. PMID:17758793 doi:http://dx.doi.org/10.1126/science.205.4405.507
- ↑ Kold D, Dauter Z, Laustsen AK, Brzozowski AM, Turkenburg JP, Nielsen AD, Koldso H, Petersen E, Schiott B, De Maria L, Wilson KS, Svendsen A, Wimmer R. Thermodynamic and structural investigation of the specific SDS binding of humicola insolens cutinase. Protein Sci. 2014 May 16. doi: 10.1002/pro.2489. PMID:24832484 doi:http://dx.doi.org/10.1002/pro.2489
