1cus
From Proteopedia
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| - | [[Image:1cus.jpg|left|200px]] | + | [[Image:1cus.jpg|left|200px]] |
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| - | '''FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT''' | + | {{Structure |
| + | |PDB= 1cus |SIZE=350|CAPTION= <scene name='initialview01'>1cus</scene>, resolution 1.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CUS is a [ | + | 1CUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_solani_subsp._pisi Fusarium solani subsp. pisi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUS OCA]. |
==Reference== | ==Reference== | ||
| - | Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent., Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C, Nature. 1992 Apr 16;356(6370):615-8. PMID:[http:// | + | Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent., Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C, Nature. 1992 Apr 16;356(6370):615-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1560844 1560844] |
[[Category: Fusarium solani subsp. pisi]] | [[Category: Fusarium solani subsp. pisi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase(serine esterase)]] | [[Category: hydrolase(serine esterase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:07 2008'' |
Revision as of 08:29, 20 March 2008
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FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT
Overview
Lipases belong to a class of esterases whose activity on triglycerides is greatly enhanced at lipid-water interfaces. This phenomenon, called interfacial activation, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic site, is displaced on substrate or inhibitor binding and probably interacts with the lipid matrix. Fusarium solani pisi cutinase belongs to a group of homologous enzymes of relative molecular mass 22-25K (ref. 7) capable of degrading cutin, the insoluble lipid-polyester matrix covering the surface of plants, and hydrolysing triglycerides. Cutinases differ from classical lipases in that they do not exhibit interfacial activation; they are active on soluble as well as on emulsified triglycerides. Cutinases therefore establish a bridge between esterases and lipases. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli. Cutinase is an alpha-beta protein; the active site is composed of the triad Ser 120, His 188 and Asp 175. Unlike other lipases, the catalytic serine is not buried under surface loops, but is accessible to solvent. This could explain why cutinase does not display interfacial activation.
About this Structure
1CUS is a Single protein structure of sequence from Fusarium solani subsp. pisi. Full crystallographic information is available from OCA.
Reference
Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent., Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C, Nature. 1992 Apr 16;356(6370):615-8. PMID:1560844
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