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1thg

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[[Image:1thg.gif|left|200px]]
 
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==1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM==
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The line below this paragraph, containing "STRUCTURE_1thg", creates the "Structure Box" on the page.
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<StructureSection load='1thg' size='340' side='right'caption='[[1thg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1thg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geotrichum_candidum Geotrichum candidum]. 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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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{{STRUCTURE_1thg| PDB=1thg | SCENE= }}
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<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>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/1thg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1thg ConSurf].
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<div style="clear:both"></div>
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'''1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM'''
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Geotrichum candidum]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Cygler M]]
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1THG is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THG OCA].
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[[Category: Schrag JD]]
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8464065 8464065]
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[[Category: Single protein]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Cygler, M.]]
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[[Category: Schrag, J D.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:57:09 2008''
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Current revision

1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM

PDB ID 1thg

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