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| | <StructureSection load='2xfg' size='340' side='right'caption='[[2xfg]], [[Resolution|resolution]] 1.68Å' scene=''> | | <StructureSection load='2xfg' size='340' side='right'caption='[[2xfg]], [[Resolution|resolution]] 1.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xfg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XFG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xfg]] is a 2 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=2XFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.679Å</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2xfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfg OCA], [http://pdbe.org/2xfg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xfg RCSB], [http://www.ebi.ac.uk/pdbsum/2xfg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfg 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=2xfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfg OCA], [https://pdbe.org/2xfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfg RCSB], [https://www.ebi.ac.uk/pdbsum/2xfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GUNI_CLOTH GUNI_CLOTH]] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Principally active against barley beta-glucan. | + | [https://www.uniprot.org/uniprot/GUNI_ACET2 GUNI_ACET2] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Principally active against barley beta-glucan. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ruminiclostridium thermocellum yutin and galperin 2013]] | + | [[Category: Acetivibrio thermocellus]] |
| - | [[Category: Cellulase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bayer, E A]] | + | [[Category: Bayer EA]] |
| - | [[Category: Burstein, T]] | + | [[Category: Burstein T]] |
| - | [[Category: Frolow, F]] | + | [[Category: Frolow F]] |
| - | [[Category: Jindou, S]] | + | [[Category: Jindou S]] |
| - | [[Category: Lamed, R]] | + | [[Category: Lamed R]] |
| - | [[Category: Petkun, S]] | + | [[Category: Petkun S]] |
| - | [[Category: Shimon, J W.L]] | + | [[Category: Shimon JWL]] |
| - | [[Category: Shoham, Y]] | + | [[Category: Shoham Y]] |
| - | [[Category: Yaniv, O]] | + | [[Category: Yaniv O]] |
| - | [[Category: Family-9 glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-sugar binding protein complex]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
GUNI_ACET2 This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Principally active against barley beta-glucan.
Publication Abstract from PubMed
Non-cellulosomal processive endoglucanase 9I (Cel9I) from Clostridium thermocellum is a modular protein, consisting of a family-9 glycoside hydrolase (GH9) catalytic module and two family-3 carbohydrate-binding modules (CBM3c and CBM3b), separated by linker regions. GH9 does not show cellulase activity when expressed without CBM3c and CBM3b and the presence of the CBM3c was previously shown to be essential for endoglucanase activity. Physical reassociation of independently expressed GH9 and CBM3c modules (containing linker sequences) restored 60-70% of the intact Cel9I endocellulase activity. However, the mechanism responsible for recovery of activity remained unclear. In this work we independently expressed recombinant GH9 and CBM3c with and without their interconnecting linker in Escherichia coli. We crystallized and determined the molecular structure of the GH9/linker-CBM3c heterodimer at a resolution of 1.68 A to understand the functional and structural importance of the mutual spatial orientation of the modules and the role of the interconnecting linker during their re-association. Enzyme activity assays and isothermal titration calorimetry were performed to study and compare the effect of the linker on the re-association. The results indicated that reassembly of the modules could also occur without the linker, albeit with only very low recovery of endoglucanase activity. We propose that the linker regions in the GH9/CBM3c endoglucanases are important for spatial organization and fixation of the modules into functional enzymes.
Reassembly and co-crystallization of a family 9 processive endoglucanase from its component parts: structural and functional significance of the intermodular linker.,Petkun S, Rozman Grinberg I, Lamed R, Jindou S, Burstein T, Yaniv O, Shoham Y, Shimon LJ, Bayer EA, Frolow F PeerJ. 2015 Sep 15;3:e1126. doi: 10.7717/peerj.1126. eCollection 2015. PMID:26401442[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Petkun S, Rozman Grinberg I, Lamed R, Jindou S, Burstein T, Yaniv O, Shoham Y, Shimon LJ, Bayer EA, Frolow F. Reassembly and co-crystallization of a family 9 processive endoglucanase from its component parts: structural and functional significance of the intermodular linker. PeerJ. 2015 Sep 15;3:e1126. doi: 10.7717/peerj.1126. eCollection 2015. PMID:26401442 doi:http://dx.doi.org/10.7717/peerj.1126
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