1thg

From Proteopedia

(Difference between revisions)

Revision as of 09:27, 29 September 2021

1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM

Structural highlights

1thg is a 1 chain structure with sequence from endomyces_geotrichum Atcc 22600 endomyces geotrichum . Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	LIP2 (ATCC 22600 Endomyces geotrichum )
Activity:	Triacylglycerol lipase, with EC number 3.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LIP2_GEOCN] Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schrag JD, Cygler M. 1.8 A refined structure of the lipase from Geotrichum candidum. J Mol Biol. 1993 Mar 20;230(2):575-91. PMID:8464065 doi:http://dx.doi.org/10.1006/jmbi.1993.1171

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1thg"

Categories: Large Structures | Triacylglycerol lipase | Cygler, M | Schrag, J D

@@ Line 3: / Line 3: @@
 <StructureSection load='1thg' size='340' side='right'caption='[[1thg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1thg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_22600_[[endomyces_geotrichum]] Atcc 22600 [[endomyces geotrichum]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1THG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1thg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_22600_[[endomyces_geotrichum]] Atcc 22600 [[endomyces geotrichum]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1THG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LIP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1173061 ATCC 22600 [[Endomyces geotrichum]]])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LIP2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1173061 ATCC 22600 [[Endomyces geotrichum]]])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thg OCA], [http://pdbe.org/1thg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1thg RCSB], [http://www.ebi.ac.uk/pdbsum/1thg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1thg ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thg OCA], [https://pdbe.org/1thg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1thg RCSB], [https://www.ebi.ac.uk/pdbsum/1thg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1thg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LIP2_GEOCN LIP2_GEOCN]] Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14).
+[[https://www.uniprot.org/uniprot/LIP2_GEOCN LIP2_GEOCN]] Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1thg

From Proteopedia

Revision as of 09:27, 29 September 2021

1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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