3dea: Difference between revisions

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-{{Seed}}
-[[Image:3dea.png|left|200px]]
-<!--
+==Glomerella cingulata PETFP-cutinase complex==
-The line below this paragraph, containing "STRUCTURE_3dea", creates the "Structure Box" on the page.
+<StructureSection load='3dea' size='340' side='right'caption='[[3dea]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3dea]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Colletotrichum_gloeosporioides Colletotrichum gloeosporioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DEA FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HZH:1,1,1-TRIFLUORO-3-[(2-PHENYLETHYL)SULFANYL]PROPAN-2-ONE'>HZH</scene></td></tr>
-{{STRUCTURE_3dea|  PDB=3dea  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dea OCA], [https://pdbe.org/3dea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dea RCSB], [https://www.ebi.ac.uk/pdbsum/3dea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dea ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CUTI1_COLGL CUTI1_COLGL] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.<ref>PMID:17043825</ref>
+== 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/de/3dea_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=3dea ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cutinase belongs to a group of enzymes that catalyze the hydrolysis of esters and triglycerides. Structural studies on the enzyme from Fusarium solani have revealed the presence of a classic catalytic triad that has been implicated in the enzyme's mechanism. We have solved the crystal structure of Glomerella cingulata cutinase in the absence and in the presence of the inhibitors E600 (diethyl p-nitrophenyl phosphate) and PETFP (3-phenethylthio-1,1,1-trifluoropropan-2-one) to resolutions between 2.6 and 1.9 A. Analysis of these structures reveals that the catalytic triad (Ser136, Asp191, and His204) adopts an unusual configuration with the putative essential histidine His204 swung out of the active site into a position where it is unable to participate in catalysis, with the imidazole ring 11 A away from its expected position. Solution-state NMR experiments are consistent with the disrupted configuration of the triad observed crystallographically. H204N, a site-directed mutant, was shown to be catalytically inactive, confirming the importance of this residue in the enzyme mechanism. These findings suggest that, during its catalytic cycle, cutinase undergoes a significant conformational rearrangement converting the loop bearing the histidine from an inactive conformation, in which the histidine of the triad is solvent exposed, to an active conformation, in which the triad assumes a classic configuration.
-===Glomerella cingulata PETFP-cutinase complex===
+Catalysis by Glomerella cingulata Cutinase Requires Conformational Cycling between the Active and Inactive States of Its Catalytic Triad.,Nyon MP, Rice DW, Berrisford JM, Hounslow AM, Moir AJ, Huang H, Nathan S, Mahadi NM, Bakar FD, Craven CJ J Mol Biol. 2008 Oct 31. PMID:18983850<ref>PMID:18983850</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3dea" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18983850}}, adds the Publication Abstract to the page
+*[[Cutinase 3D structures|Cutinase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18983850 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18983850}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Colletotrichum gloeosporioides]]
-DEA is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Glomerella_cingulata Glomerella cingulata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DEA OCA].
+[[Category: Large Structures]]
+[[Category: Berrisford JM]]
-==Reference==
+[[Category: Craven CJ]]
-Catalysis by Glomerella cingulata Cutinase Requires Conformational Cycling between the Active and Inactive States of Its Catalytic Triad., Nyon MP, Rice DW, Berrisford JM, Hounslow AM, Moir AJ, Huang H, Nathan S, Mahadi NM, Bakar FD, Craven CJ, J Mol Biol. 2008 Oct 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18983850 18983850]
+[[Category: Farah Diba AB]]
-[[Category: Cutinase]]
+[[Category: Hounslow AM]]
-[[Category: Glomerella cingulata]]
+[[Category: Huang H]]
-[[Category: Berrisford, J M.]]
+[[Category: Mahadi NM]]
-[[Category: Craven, C J.]]
+[[Category: Moir AJG]]
-[[Category: Diba, A B.Farah.]]
+[[Category: Nathan S]]
-[[Category: Hounslow, A M.]]
+[[Category: Nyon MP]]
-[[Category: Huang, H.]]
+[[Category: Rice DW]]
-[[Category: Mahadi, N M.]]
-[[Category: Moir, A J.G.]]
-[[Category: Nathan, S.]]
-[[Category: Nyon, M P.]]
-[[Category: Rice, D W.]]
-[[Category: Catalytic triad]]
-[[Category: Hydrolase]]
-[[Category: Secreted]]
-[[Category: Serine esterase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan  7 08:10:13 2009''