5tgl: Difference between revisions

Line 1:

[[Image:5tgl.gif|left|200px]]<br /><applet load="5tgl" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:5tgl.gif|left|200px]]<br /><applet load="5tgl" size="350" color="white" frame="true" align="right" spinBox="true"

caption="5tgl, resolution 3.0Å" />

'''A MODEL FOR INTERFACIAL ACTIVATION IN LIPASES FROM THE STRUCTURE OF A FUNGAL LIPASE-INHIBITOR COMPLEX'''<br />

==Overview==

Lipases are hydrolytic enzymes which break down triacylglycerides into, free fatty acids and glycerols. They have been classified as serine, hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate., Lipase activity is greatly increased at the lipid-water interface, a, phenomenon known as interfacial activation. X-ray analysis has revealed, the atomic structures of two triacylglycerol lipases, unrelated in, sequence: the human pancreatic lipase (hPL)4, and an enzyme isolated from, the fungus Rhizomucor (formerly Mucor) miehei (RmL). In both enzymes the, active centres contain structurally analogous Asp-His-Ser triads, (characteristic of serine proteinases), which are buried completely, beneath a short helical segment, or 'lid'. Here we present the crystal, structure (at 3 A resolution) of a complex of R. miehei lipase with, n-hexylphosphonate ethyl ester in which the enzyme's active site is, exposed by the movement of the helical lid. This movement also increases, the nonpolarity of the surface surrounding the catalytic site. We propose, that the structure of the enzyme in this complex is equivalent to the, activated state generated by the oil-water interface.

Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. They have been classified as serine hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate. Lipase activity is greatly increased at the lipid-water interface, a phenomenon known as interfacial activation. X-ray analysis has revealed the atomic structures of two triacylglycerol lipases, unrelated in sequence: the human pancreatic lipase (hPL)4, and an enzyme isolated from the fungus Rhizomucor (formerly Mucor) miehei (RmL). In both enzymes the active centres contain structurally analogous Asp-His-Ser triads (characteristic of serine proteinases), which are buried completely beneath a short helical segment, or 'lid'. Here we present the crystal structure (at 3 A resolution) of a complex of R. miehei lipase with n-hexylphosphonate ethyl ester in which the enzyme's active site is exposed by the movement of the helical lid. This movement also increases the nonpolarity of the surface surrounding the catalytic site. We propose that the structure of the enzyme in this complex is equivalent to the activated state generated by the oil-water interface.

==About this Structure==

5TGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhizomucor_miehei Rhizomucor miehei] with HEE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=5TGL OCA].

5TGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhizomucor_miehei Rhizomucor miehei] with <scene name='pdbligand=HEE:'>HEE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TGL OCA].

==Reference==

Line 15:

[[Category: Triacylglycerol lipase]]

[[Category: Bjorkling, F.]]

[[Category: Brzozowski, A.M.]]

[[Category: Brzozowski, A M.]]

[[Category: Derewenda, U.]]

[[Category: Derewenda, Z.S.]]

[[Category: Derewenda, Z S.]]

[[Category: Dodson, G.G.]]

[[Category: Dodson, G G.]]

[[Category: Huge-Jensen, B.]]

[[Category: Lawson, D.]]

[[Category: Patkar, S.R.]]

[[Category: Patkar, S R.]]

[[Category: Thim, L.]]

[[Category: Turkenburg, J.P.]]

[[Category: Turkenburg, J P.]]

[[Category: HEE]]

[[Category: hydrolase(carboxylic esterase)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 19:42:~~16 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:5tgl.gif|left|200px]]<br /><applet load="5tgl" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:5tgl.gif|left|200px]]<br /><applet load="5tgl" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="5tgl, resolution 3.0&Aring;" />
 '''A MODEL FOR INTERFACIAL ACTIVATION IN LIPASES FROM THE STRUCTURE OF A FUNGAL LIPASE-INHIBITOR COMPLEX'''<br />
 ==Overview==
-Lipases are hydrolytic enzymes which break down triacylglycerides into, free fatty acids and glycerols. They have been classified as serine, hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate., Lipase activity is greatly increased at the lipid-water interface, a, phenomenon known as interfacial activation. X-ray analysis has revealed, the atomic structures of two triacylglycerol lipases, unrelated in, sequence: the human pancreatic lipase (hPL)4, and an enzyme isolated from, the fungus Rhizomucor (formerly Mucor) miehei (RmL). In both enzymes the, active centres contain structurally analogous Asp-His-Ser triads, (characteristic of serine proteinases), which are buried completely, beneath a short helical segment, or 'lid'. Here we present the crystal, structure (at 3 A resolution) of a complex of R. miehei lipase with, n-hexylphosphonate ethyl ester in which the enzyme's active site is, exposed by the movement of the helical lid. This movement also increases, the nonpolarity of the surface surrounding the catalytic site. We propose, that the structure of the enzyme in this complex is equivalent to the, activated state generated by the oil-water interface.
+Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. They have been classified as serine hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate. Lipase activity is greatly increased at the lipid-water interface, a phenomenon known as interfacial activation. X-ray analysis has revealed the atomic structures of two triacylglycerol lipases, unrelated in sequence: the human pancreatic lipase (hPL)4, and an enzyme isolated from the fungus Rhizomucor (formerly Mucor) miehei (RmL). In both enzymes the active centres contain structurally analogous Asp-His-Ser triads (characteristic of serine proteinases), which are buried completely beneath a short helical segment, or 'lid'. Here we present the crystal structure (at 3 A resolution) of a complex of R. miehei lipase with n-hexylphosphonate ethyl ester in which the enzyme's active site is exposed by the movement of the helical lid. This movement also increases the nonpolarity of the surface surrounding the catalytic site. We propose that the structure of the enzyme in this complex is equivalent to the activated state generated by the oil-water interface.
 ==About this Structure==
-TGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhizomucor_miehei Rhizomucor miehei] with HEE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5TGL OCA].
+TGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhizomucor_miehei Rhizomucor miehei] with <scene name='pdbligand=HEE:'>HEE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TGL OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Triacylglycerol lipase]]
 [[Category: Bjorkling, F.]]
-[[Category: Brzozowski, A.M.]]
+[[Category: Brzozowski, A M.]]
 [[Category: Derewenda, U.]]
-[[Category: Derewenda, Z.S.]]
+[[Category: Derewenda, Z S.]]
-[[Category: Dodson, G.G.]]
+[[Category: Dodson, G G.]]
 [[Category: Huge-Jensen, B.]]
 [[Category: Lawson, D.]]
-[[Category: Patkar, S.R.]]
+[[Category: Patkar, S R.]]
 [[Category: Thim, L.]]
-[[Category: Turkenburg, J.P.]]
+[[Category: Turkenburg, J P.]]
 [[Category: HEE]]
 [[Category: hydrolase(carboxylic esterase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:42:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:51 2008''