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| | <StructureSection load='1nlr' size='340' side='right'caption='[[1nlr]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='1nlr' size='340' side='right'caption='[[1nlr]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nlr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NLR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nlr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NLR FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nlr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlr OCA], [http://pdbe.org/1nlr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nlr RCSB], [http://www.ebi.ac.uk/pdbsum/1nlr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nlr ProSAT]</span></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=1nlr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlr OCA], [https://pdbe.org/1nlr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nlr RCSB], [https://www.ebi.ac.uk/pdbsum/1nlr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nlr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q54331_STRLI Q54331_STRLI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/1nlr_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/1nlr_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces lividans krasil'nikov et al. 1965]] | |
| - | [[Category: Cellulase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davies, G J]] | + | [[Category: Streptomyces lividans]] |
| - | [[Category: Dupont, C]] | + | [[Category: Davies GJ]] |
| - | [[Category: Sulzenbacher, G]] | + | [[Category: Dupont C]] |
| - | [[Category: Celb2]] | + | [[Category: Sulzenbacher G]] |
| - | [[Category: Endoglucanase]]
| + | |
| - | [[Category: Family 12]]
| + | |
| - | [[Category: Glycosyl hydrolase]]
| + | |
| Structural highlights
Function
Q54331_STRLI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cellulases are the glycoside hydrolases responsible for the enzymatic breakdown of the structural plant polymer cellulose. Together with xylanases they counteract the lmitless accumulation of plant biomass in nature and are of considerable fundamental and biotechnological interest. Endoglucanase CelB from Streptomyces lividans performs hydrolysis of the beta-1,4-glycosidic bonds of cellulose, with net retention of anomeric configuration. The enzyme is a member of glycoside hydrolase family 12 [Henrissat, B., and Bairoch, A. (1996) Biochem. J. 316, 695-696], which had previously eluded detailed structural analysis. A truncated, but cataytically competent form of CelB, locking the flexible linker region and cellulose-binding domain, has been constructed and overexpressed in a S. lividans expression system. The three-dimensional X-ray structure of the resulting catalytic domain, CelB2, has been solved by conventional multiple isomorphous replacement methods and refined to an R factor of 0.187 at 1.75 A resolution. The overall fold of the enzyme shows a remarkable similarity to that of family 11 xylanases, as previously predicted by hydrophobic clustering analysis [Torronen, A., Kubicek, C.P., and Henrissat, B. (1993) FEBS Lett. 321, 135-139]. The 23 kDa protein presents a jelly-roll topology, built up mainly by antiparallel beta-sheets arranged in a sandwich-like manner. A deep substrate-binding cleft runs across the surface, as has been observed in other endoglucanase structures, and is potentially able to accommodate up to five binding subsites. The likely catalytic nucleophile and Bronsted acid/base, residues Glu 120 and Glue 203, respectively, have their carboxylate groups separated by a distance of approximately 7.0 A and are located approximately 15 A from one end of the cleft, implying a -3 to +2 active site.
The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution.,Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ Biochemistry. 1997 Dec 23;36(51):16032-9. PMID:9440876[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ. The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution. Biochemistry. 1997 Dec 23;36(51):16032-9. PMID:9440876 doi:10.1021/bi972407v
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