2cut
From Proteopedia
(New page: 200px<br /><applet load="2cut" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cut, resolution 1.9Å" /> '''CUTINASE, A LIPOLYTIC...) |
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| - | [[Image:2cut.jpg|left|200px]]<br /><applet load="2cut" size=" | + | [[Image:2cut.jpg|left|200px]]<br /><applet load="2cut" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cut, resolution 1.9Å" /> | caption="2cut, resolution 1.9Å" /> | ||
'''CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED OXYANION HOLE'''<br /> | '''CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED OXYANION HOLE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cutinases, a group of cutin degrading enzymes with molecular masses of | + | Cutinases, a group of cutin degrading enzymes with molecular masses of around 22-25 kDa (Kolattukudy, 1984), are also able to efficiently hydrolyse triglycerides (De Geus et al., 1989; Lauwereys et al., 1991), but without exhibiting the interfacial activation phenomenom (Sarda et al., 1958). They belong to a class of proteins with a common structural framework, called the alpha/beta hydrolase fold (Martinez et al., 1992; Ollis et al., 1992). We describe herein the structure of cutinase covalently inhibited by diethyl-p-nitrophenyl phosphate (E600) and refined at 1.9-A resolution. Contrary to what has previously been reported with lipases (Brzozowski et al., 1991; Derewenda et al., 1992; Van Tilbeurgh et al., 1993), no significant structural rearrangement was observed here in cutinase upon the inhibitor binding. Moreover, the structure of the active site machinery, consisting of a catalytic triad (S120, H188, D175) and an oxyanion hole (Q121 and S42), was found to be identical to that of the native enzyme, whereas the oxyanion hole of Rhizomucor lipase (Brzozowski et al., 1991; Derewenda et al., 1992), like that of pancreatic lipase (van Tilbeurgh et al., 1993), is formed only upon enzyme-ligand complex formation. The fact that cutinase does not display interfacial activation cannot therefore only be due to the absence of a lid but might also be attributable to the presence of a preformed oxyanion hole. |
==About this Structure== | ==About this Structure== | ||
| - | 2CUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nectria_haematococca Nectria haematococca] with DEP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2CUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nectria_haematococca Nectria haematococca] with <scene name='pdbligand=DEP:'>DEP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CUT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: complex(serine esterase/inhibitor)]] | [[Category: complex(serine esterase/inhibitor)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:42 2008'' |
Revision as of 14:52, 21 February 2008
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CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED OXYANION HOLE
Overview
Cutinases, a group of cutin degrading enzymes with molecular masses of around 22-25 kDa (Kolattukudy, 1984), are also able to efficiently hydrolyse triglycerides (De Geus et al., 1989; Lauwereys et al., 1991), but without exhibiting the interfacial activation phenomenom (Sarda et al., 1958). They belong to a class of proteins with a common structural framework, called the alpha/beta hydrolase fold (Martinez et al., 1992; Ollis et al., 1992). We describe herein the structure of cutinase covalently inhibited by diethyl-p-nitrophenyl phosphate (E600) and refined at 1.9-A resolution. Contrary to what has previously been reported with lipases (Brzozowski et al., 1991; Derewenda et al., 1992; Van Tilbeurgh et al., 1993), no significant structural rearrangement was observed here in cutinase upon the inhibitor binding. Moreover, the structure of the active site machinery, consisting of a catalytic triad (S120, H188, D175) and an oxyanion hole (Q121 and S42), was found to be identical to that of the native enzyme, whereas the oxyanion hole of Rhizomucor lipase (Brzozowski et al., 1991; Derewenda et al., 1992), like that of pancreatic lipase (van Tilbeurgh et al., 1993), is formed only upon enzyme-ligand complex formation. The fact that cutinase does not display interfacial activation cannot therefore only be due to the absence of a lid but might also be attributable to the presence of a preformed oxyanion hole.
About this Structure
2CUT is a Single protein structure of sequence from Nectria haematococca with as ligand. Full crystallographic information is available from OCA.
Reference
Cutinase, a lipolytic enzyme with a preformed oxyanion hole., Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C, Biochemistry. 1994 Jan 11;33(1):83-9. PMID:8286366
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