1thg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1thg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1thg, resolution 1.8&Aring;" /> '''1.8 ANGSTROMS REFINED...)
Current revision (07:37, 23 October 2024) (edit) (undo)
 
(20 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1thg.gif|left|200px]]<br /><applet load="1thg" size="450" 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==
+
==1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM==
-
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.
+
<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 [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>
 +
</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>
 +
<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>
 +
<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 ==
 +
[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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/1thg_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
==About this Structure==
+
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<ref>PMID:8464065</ref>
-
1THG 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].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8464065 8464065]
+
</div>
-
[[Category: Single protein]]
+
<div class="pdbe-citations 1thg" style="background-color:#fffaf0;"></div>
-
[[Category: Triacylglycerol lipase]]
+
-
[[Category: Cygler, M.]]
+
-
[[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''
+
==See Also==
 +
*[[Lipase 3D Structures|Lipase 3D Structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Geotrichum candidum]]
 +
[[Category: Large Structures]]
 +
[[Category: Cygler M]]
 +
[[Category: Schrag JD]]

Current revision

1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM

PDB ID 1thg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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