1thg: Difference between revisions

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1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM

OverviewOverview

A lipase from the fungus Geotrichum candidum is one of only three interfacially activated lipases whose structures have been reported to date. We have previously reported the partially refined 2.2 A structure of this enzyme. We have subsequently extended the resolution and here report the fully refined 1.8 A structure of this lipase. The structure observed in the crystal is apparently not the lipolytic conformation, as the active site is not accessible from the surface of the molecule. A single large cavity is found in the interior of the molecule and extends from the catalytic Ser to two surface helices, suggesting that this face may be the region that interacts with the lipid interface. The mobility of local segments on this face is indicated by temperature factors larger than elsewhere in the molecule and by the observation of several residues whose side-chains are discretely disordered. These observations strongly suggest that this portion of the molecule is involved in interfacial and substrate binding, but the exact nature of the conformational changes induced by binding to the lipid interface can not be determined.

About this StructureAbout this Structure

1THG is a Single protein structure of sequence from [1] with and as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.

ReferenceReference

1.8 A refined structure of the lipase from Geotrichum candidum., Schrag JD, Cygler M, J Mol Biol. 1993 Mar 20;230(2):575-91. PMID:8464065

Page seeded by OCA on Thu Feb 21 15:13:31 2008

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OCA

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-[[Image:1thg.gif|left|200px]]<br /><applet load="1thg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1thg.gif|left|200px]]<br /><applet load="1thg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1thg, resolution 1.8&Aring;" />
 '''1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM'''<br />
 ==Overview==
-A lipase from the fungus Geotrichum candidum is one of only three, interfacially activated lipases whose structures have been reported to, date. We have previously reported the partially refined 2.2 A structure of, this enzyme. We have subsequently extended the resolution and here report, the fully refined 1.8 A structure of this lipase. The structure observed, in the crystal is apparently not the lipolytic conformation, as the active, site is not accessible from the surface of the molecule. A single large, cavity is found in the interior of the molecule and extends from the, catalytic Ser to two surface helices, suggesting that this face may be the, region that interacts with the lipid interface. The mobility of local, segments on this face is indicated by temperature factors larger than, elsewhere in the molecule and by the observation of several residues whose, side-chains are discretely disordered. These observations strongly suggest, that this portion of the molecule is involved in interfacial and substrate, binding, but the exact nature of the conformational changes induced by, binding to the lipid interface can not be determined.
+A lipase from the fungus Geotrichum candidum is one of only three interfacially activated lipases whose structures have been reported to date. We have previously reported the partially refined 2.2 A structure of this enzyme. We have subsequently extended the resolution and here report the fully refined 1.8 A structure of this lipase. The structure observed in the crystal is apparently not the lipolytic conformation, as the active site is not accessible from the surface of the molecule. A single large cavity is found in the interior of the molecule and extends from the catalytic Ser to two surface helices, suggesting that this face may be the region that interacts with the lipid interface. The mobility of local segments on this face is indicated by temperature factors larger than elsewhere in the molecule and by the observation of several residues whose side-chains are discretely disordered. These observations strongly suggest that this portion of the molecule is involved in interfacial and substrate binding, but the exact nature of the conformational changes induced by binding to the lipid interface can not be determined.
 ==About this Structure==
-THG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAG and NDG as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1THG OCA].
+THG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1THG OCA].
 ==Reference==
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 [[Category: Triacylglycerol lipase]]
 [[Category: Cygler, M.]]
-[[Category: Schrag, J.D.]]
+[[Category: Schrag, J D.]]
 [[Category: NAG]]
 [[Category: NDG]]
 [[Category: hydrolase(carboxylic esterase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:16:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:31 2008''