6cel: Difference between revisions

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-{{Seed}}
-[[Image:6cel.png|left|200px]]
-<!--
+==CBH1 (E212Q) CELLOPENTAOSE COMPLEX==
-The line below this paragraph, containing "STRUCTURE_6cel", creates the "Structure Box" on the page.
+<StructureSection load='6cel' size='340' side='right'caption='[[6cel]], [[Resolution|resolution]] 1.70&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'>[[6cel]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CEL 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]] 1.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</scene>, <scene name='pdbligand=PRD_900016:beta-cellopentaose'>PRD_900016</scene></td></tr>
-{{STRUCTURE_6cel|  PDB=6cel  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cel OCA], [https://pdbe.org/6cel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cel RCSB], [https://www.ebi.ac.uk/pdbsum/6cel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cel ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
+== 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/ce/6cel_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=6cel ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Detailed information has been obtained, by means of protein X-ray crystallography, on how a cellulose chain is bound in the cellulose-binding tunnel of cellobiohydrolase I (CBHI), the major cellulase in the hydrolysis of native, crystalline cellulose by the fungus Trichoderma reesei. Three high-resolution crystal structures of different catalytically deficient mutants of CBHI in complex with cellotetraose, cellopentaose and cellohexaose have been refined at 1.9, 1.7 and 1.9 A resolution, respectively. The observed binding of cellooligomers in the tunnel allowed unambiguous identification of ten well-defined subsites for glucosyl units that span a length of approximately 50 A. All bound oligomers have the same directionality and orientation, and the positions of the glucosyl units in each binding site agree remarkably well between the different complexes. The binding mode observed here corresponds to that expected during productive binding of a cellulose chain. The structures support the hypothesis that hydrolysis by CBHI proceeds from the reducing towards the non-reducing end of a cellulose chain, and they provide a structural explanation for the observed distribution of initial hydrolysis products.
-===CBH1 (E212Q) CELLOPENTAOSE COMPLEX===
+High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei.,Divne C, Stahlberg J, Teeri TT, Jones TA J Mol Biol. 1998 Jan 16;275(2):309-25. PMID:9466911<ref>PMID:9466911</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6cel" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9466911}}, adds the Publication Abstract to the page
+*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9466911 is the PubMed ID number.
+*[[Glucanase 3D structures|Glucanase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_9466911}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-CEL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CEL OCA].
+[[Category: Large Structures]]
+[[Category: Trichoderma reesei]]
-==Reference==
+[[Category: Divne C]]
-High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei., Divne C, Stahlberg J, Teeri TT, Jones TA, J Mol Biol. 1998 Jan 16;275(2):309-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9466911 9466911]
+[[Category: Jones TA]]
-[[Category: Cellulose 1,4-beta-cellobiosidase]]
+[[Category: Stahlberg J]]
-[[Category: Hypocrea jecorina]]
-[[Category: Single protein]]
-[[Category: Divne, C.]]
-[[Category: Jones, T A.]]
-[[Category: Stahlberg, J.]]
-[[Category: Cellulose degradation]]
-[[Category: Glycoprotein]]
-[[Category: Glycosidase]]
-[[Category: Glycosylated protein]]
-[[Category: Hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 14:15:35 2008''