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| - | [[Image:1cem.jpg|left|200px]] | |
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| - | {{Structure
| + | ==ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395== |
| - | |PDB= 1cem |SIZE=350|CAPTION= <scene name='initialview01'>1cem</scene>, resolution 1.65Å
| + | <StructureSection load='1cem' size='340' side='right'caption='[[1cem]], [[Resolution|resolution]] 1.65Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1cem]] 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=1CEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEM FirstGlance]. <br> |
| - | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | |GENE= CELA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cem OCA], [https://pdbe.org/1cem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cem RCSB], [https://www.ebi.ac.uk/pdbsum/1cem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cem ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY=
| + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cem OCA], [http://www.ebi.ac.uk/pdbsum/1cem PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cem RCSB]</span>
| + | [https://www.uniprot.org/uniprot/GUNA_ACET2 GUNA_ACET2] 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/1cem_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=1cem ConSurf]. |
| | + | <div style="clear:both"></div> |
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| - | '''ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395'''
| + | ==See Also== |
| - | | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | BACKGROUND. Cellulases, which catalyze the hydrolysis of glycosidic bonds in cellulose, can be classified into several different protein families. Endoglucanase CelA is a member of glycosyl hydrolase family 8, a family for which no structural information was previously available. RESULTS. The crystal structure of CelA was determined by multiple isomorphous replacement and refined to 1.65 A resolution. The protein folds into a regular (alpha/alpha)6 barrel formed by six inner and six outer alpha helices. Cello-oligosaccharides bind to an acidic cleft containing at least five D-glucosyl-binding subsites (A-E) such that the scissile glycosidic linkage lies between subsites C and D. The strictly conserved residue Glu95, which occupies the center of the substrate-binding cleft and is hydrogen bonded to the glycosidic oxygen, has been assigned the catalytic role of proton donor. CONCLUSIONS. The present analysis provides a basis for modeling homologous family 8 cellulases. The architecture of the active-site cleft, presenting at least five glucosyl-binding subsites, explains why family 8 cellulases cleave cello-oligosaccharide polymers that are at least five D-glycosyl subunits long. Furthermore, the structure of CelA allows comparison with (alpha/alpha)6 barrel glycosidases that are not related in sequence, suggesting a possible, albeit distant, evolutionary relationship between different families of glycosyl hydrolases.
| + | [[Category: Acetivibrio thermocellus]] |
| - | | + | [[Category: Large Structures]] |
| - | ==About this Structure==
| + | [[Category: Alzari PM]] |
| - | 1CEM 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=1CEM OCA].
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| - | | + | |
| - | ==Reference==
| + | |
| - | The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum., Alzari PM, Souchon H, Dominguez R, Structure. 1996 Mar 15;4(3):265-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8805535 8805535]
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| - | [[Category: Cellulase]] | + | |
| - | [[Category: Clostridium thermocellum]] | + | |
| - | [[Category: Single protein]]
| + | |
| - | [[Category: Alzari, P M.]] | + | |
| - | [[Category: cellulase]]
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| - | [[Category: clostridium thermocellum]]
| + | |
| - | [[Category: family d/8 of glycosyl hydrolase]]
| + | |
| - | [[Category: glycosyl hydrolase]]
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| - | [[Category: glycosyltransferase]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:14 2008''
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