SMART: Cutinase domain annotation

Cutinase

SMART accession number:	SM01110
Description:	This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase. Aerial plant organs are protected by a cuticle composed of an insoluble polymeric structural compound, cutin, which is a polyester composed of hydroxy and hydroxyepoxy fatty acids. Plant pathogenic fungi produce extracellular degradative enzymes that play an important role in pathogenesis. They include cutinase, which hydrolyses cutin, facilitating fungus penetration through the cuticle. Inhibition of the enzyme can prevent fungal infection through intact cuticles. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore, the mechanism for which process is as yet unknown. (PMID 1557023)
Family alignment:	View or

There are 449 Cutinase domains in 449 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Cutinase domain is also avaliable.

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Cellular role (predicted cellular role)
Cellular role: interaction
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- 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; 268: 779-99
- Display abstract
- X-ray data have been recorded to 1.0 A resolution from a crystal of Fusariumsolani cutinase using synchrotron radiation and an imaging-plate scanner. Theanisotropic treatment of thermal motion led to a fivefold increase in accuracyand to a considerable quality improvement in the electron density maps withrespect to an intermediate isotropic model. The final model has an R-factor of9.4%, with a mean coordinate error of 0.021 A, as estimated from inversion of theleast-squares matrix. The availability of an accurate structure at atomicresolution and of meaningful estimates of the errors in its atomic parameters,allowed an extensive analysis of several stereochemical parameters, such aspeptide planarity, main-chain and some side-chain bond distances. The hydrogenatoms could be clearly identified in the electron density, thus providingunambiguous evidence on the protonation state of the catalytic histidine residue.The atomic resolution revealed an appreciable extent of flexibility in thecutinase active site, which might be correlated with a possible adaptation todifferent substrates. The anisotropic treatment of thermal factors providedinsights into the anisotropic nature of motions. The analysis of these motions inthe two loops delimiting the catalytic crevice pointed out a "breath-like"movement in the substrate binding region of cutinase.
Structure (3D structures containing this domain)

3D Structures of Cutinase domains in PDB

PDB code	Main view	Title
1agy		The 1.15 angstrom refined structure of fusarium solani pisi cutinase
1bs9		Acetylxylan esterase from p. purpurogenum refined at 1.10 angstroms
1cex		Structure of cutinase
1cua		Cutinase, n172k mutant
1cub		Cutinase, n172k, r196d mutant, monoclinic crystal form
1cuc		Cutinase, n172k, r196d mutant, orthorhombic crystal form
1cud		Cutinase, n172k, r196d mutant, monoclinic crystal form with three molecules per asymmetric unit
1cue		Cutinase, q121l mutant
1cuf		Cutinase, r156l mutant
1cug		Cutinase, r17e, n172k mutant
1cuh		Cutinase, r196e mutant
1cui		Cutinase, s120a mutant
1cuj		Cutinase, s120c mutant
1cus		Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
1cuu		Cutinase, a199c mutant
1cuv		Cutinase, a85f mutant
1cuw		Cutinase, g82a, a85f, v184i, a185l, l189f mutant
1cux		Cutinase, l114y mutant
1cuy		Cutinase, l189f mutant
1cuz		Cutinase, l81g, l182g mutant
1ffa		Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state
1ffb		Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state
1ffc		Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state
1ffd		Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state
1ffe		Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state
1g66		Acetylxylan esterase at 0.90 angstrom resolution
1oxm		Structure of cutinase
1qoz		Catalytic core domain of acetyl xylan esterase from trichoderma reesei
1xza		Fusarium solani cutinase mutant with ser 129 replaced by cys
1xzb		Fusarium solani cutinase mutant with ser 129 replaced by cys complex with mercury acetate
1xzc		Fusarium solani cutinase mutant with ser 129 replaced by cys complex with para-sulfurousphenyl mercury
1xzd		Fusarium solani cutinase mutant with ser 213 replaced by cys
1xze		Fusarium solani cutinase mutant with ser 92 replaced by cys
1xzf		Fusarium solani cutinase mutant with thr 144 replaced by cys
1xzg		Fusarium solani cutinase mutant with thr 45 replaced by ala
1xzh		Fusarium solani cutinase mutant with thr 80 replaced by pro
1xzi		Fusarium solani cutinase mutant with thr 119 replaced by his
1xzj		Fusarium solani cutinase mutant with thr 38 replaced by phe
1xzk		Fusarium solani cutinase complex with di(isopropyl)phosphate
1xzl		Fusarium solani cutinase complex with n-hexylphosphonate ethyl ester
1xzm		Fusarium solani cutinase complex with n-undecyl o-methyl chloro phosphonate ester
2axe		Iodinated complex of acetyl xylan esterase at 1.80 angstroms
2cut		Cutinase, a lipolytic enzyme with a preformed oxyanion hole
2czq		A novel cutinase-like protein from cryptococcus sp.
3dcn		Glomerella cingulata apo cutinase
3dd5		Glomerella cingulata e600-cutinase complex
3dea		Glomerella cingulata petfp-cutinase complex
3ef3		Cut-1a; ncn-pt-pincer-cutinase hybrid
3esa		Cut-1b; ncn-pt-pincer-cutinase hybrid
3esb		Cut-1c; ncn-pt-pincer-cutinase hybrid
3esc		Cut-2a; ncn-pt-pincer-cutinase hybrid
3esd		Cut-2b; ncn-pt-pincer-cutinase hybrid
3gbs		Crystal structure of aspergillus oryzae cutinase

Links (links to other resources describing this domain)
PFAM Cutinase