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| - | [[Image:1ceo.gif|left|200px]] | |
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| - | <!-- | + | ==CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN== |
| - | The line below this paragraph, containing "STRUCTURE_1ceo", creates the "Structure Box" on the page.
| + | <StructureSection load='1ceo' size='340' side='right'caption='[[1ceo]], [[Resolution|resolution]] 1.90Å' 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'>[[1ceo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEO 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]] 1.9Å</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=1ceo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ceo OCA], [https://pdbe.org/1ceo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ceo RCSB], [https://www.ebi.ac.uk/pdbsum/1ceo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ceo ProSAT]</span></td></tr> |
| - | {{STRUCTURE_1ceo| PDB=1ceo | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GUNC_ACETH GUNC_ACETH] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| | + | == 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/1ceo_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ceo ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN'''
| + | ==See Also== |
| - | | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | The structures of the Glu140-->Gln mutant of the Clostridium thermocellum endoglucanase CelC in unliganded form (CelC(E140Q)) and in complex with cellohexaose (CelC(E140Q)-Gl(C6)) have been refined to crystallographic R-factors of 19.4% at 1.9 A and 17.8% at 2.3 A resolution, respectively. The structure of CelC(E140Q)-Gl(C6) complex shows two D-glucosyl residues bound to the non-reducing end of the substrate-binding cleft. Comparison of the unliganded and complexes structures reveals conformational changes due to substrate binding, including a significant reorientation of the loop 138-141 which carries the general acid/base catalyst Glu140 in wild-type CelC. Endoglucanase CelC, a family 5 glycohydrolase, exhibits a (beta/alpha)8-fold with an additional subdomain of 54 amino acids inserted between beta-strand 6 and alpha-helix 6. Seven amino acid residues (Arg46, His90, Asn139, Glu140, His198, Tyr200, and Glu280) located close to the catalytic reaction center are strictly conserved in family 5 cellulases. Only three of these residues (His90, Gln140 and Glu280) make direct contacts with the substrate, but all participate in a network of hydrogen bonds which contribute to the stability of the active site architecture and may influence the protonation state of the two catalytic residues. Residue Trp313, which interacts with the nucleophile Glu280 and is within hydrogen bonding distance of the substrate, is involved in a non-proline cis-peptide bond. An aromatic residue occurs at an equivalent position in many other (beta/alpha)8-barrel glycosidases; the presence of a cis-peptide bond at this position in the structures of family 1 beta-glucosidases, family 2 beta-galactosidases, family 5 cellulases, family 17 beta-glucanases, and family 18 chitinases provides further evidence of an evolutionary relationship between glycosyl hydrolases with a (beta/alpha)8- architecture.
| + | [[Category: Acetivibrio thermocellus]] |
| - | | + | [[Category: Large Structures]] |
| - | ==About this Structure==
| + | [[Category: Alzari PM]] |
| - | 1CEO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEO OCA].
| + | [[Category: Dominguez R]] |
| - | | + | |
| - | ==Reference==
| + | |
| - | The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism., Dominguez R, Souchon H, Lascombe M, Alzari PM, J Mol Biol. 1996 Apr 19;257(5):1042-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8632467 8632467]
| + | |
| - | [[Category: Cellulase]] | + | |
| - | [[Category: Clostridium thermocellum]] | + | |
| - | [[Category: Single protein]]
| + | |
| - | [[Category: Alzari, P M.]] | + | |
| - | [[Category: Dominguez, R.]] | + | |
| - | [[Category: Cellulase]]
| + | |
| - | [[Category: Clostridium thermocellum]]
| + | |
| - | [[Category: Family a/5 of glycosyl hydrolase]]
| + | |
| - | [[Category: Glycosyl hydrolase]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:39:02 2008''
| + | |
