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| | <StructureSection load='4a3h' size='340' side='right'caption='[[4a3h]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='4a3h' size='340' side='right'caption='[[4a3h]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a3h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700163 Atcc 700163]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A3H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a3h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salipaludibacillus_agaradhaerens Salipaludibacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DCB:2,4-DINITROPHENYL-2-DEOXY-2-FLUORO-BETA-D-CELLOBIOSIDE'>DCB</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]] 1.65Å</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=DCB:2,4-DINITROPHENYL-2-DEOXY-2-FLUORO-BETA-D-CELLOBIOSIDE'>DCB</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=4a3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3h OCA], [http://pdbe.org/4a3h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a3h RCSB], [http://www.ebi.ac.uk/pdbsum/4a3h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3h 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=4a3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3h OCA], [https://pdbe.org/4a3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3h RCSB], [https://www.ebi.ac.uk/pdbsum/4a3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GUN5_SALAG GUN5_SALAG] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Glucanase|Glucanase]] | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 700163]] | + | [[Category: Large Structures]] |
| - | [[Category: Cellulase]] | + | [[Category: Salipaludibacillus agaradhaerens]] |
| - | [[Category: Andersen, K]] | + | [[Category: Andersen K]] |
| - | [[Category: Brzozowski, A M]] | + | [[Category: Brzozowski AM]] |
| - | [[Category: Davies, G J]] | + | [[Category: Davies GJ]] |
| - | [[Category: Mackenzie, L]] | + | [[Category: Mackenzie L]] |
| - | [[Category: Schulein, M]] | + | [[Category: Schulein M]] |
| - | [[Category: Withers, S G]] | + | [[Category: Withers SG]] |
| - | [[Category: Cellulose degradation]]
| + | |
| - | [[Category: Distortion]]
| + | |
| - | [[Category: Endoglucanase]]
| + | |
| - | [[Category: Glycoside hydrolase family 5]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Michaelis complex. skew-boat]]
| + | |
| Structural highlights
Function
GUN5_SALAG
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
The enzymatic hydrolysis of O-glycosidic linkages is one of the most diverse and widespread reactions in nature and involves a classic "textbook" enzyme mechanism. A multidisciplinary analysis of a beta-glycoside hydrolase, the Cel5A from Bacillus agaradhaerens, is presented in which the structures of each of the native, substrate, covalent-intermediate, and product complexes have been determined and their interconversions analyzed kinetically, providing unprecedented insights into the mechanism of this enzyme class. Substrate is bound in a distorted 1S3 skew-boat conformation, thereby presenting the anomeric carbon appropriately for nucleophilic attack as well as satisfying the stereoelectronic requirements for an incipient oxocarbenium ion. Leaving group departure results in the trapping of a covalent alpha-glycosyl-enzyme intermediate in which the sugar adopts an undistorted 4C1 conformation. Finally, hydrolysis of this intermediate yields a product complex in which the sugar is bound in a partially disordered mode, consistent with unfavorable interactions and low product affinity.
Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase.,Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG Biochemistry. 1998 Aug 25;37(34):11707-13. PMID:9718293[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG. Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase. Biochemistry. 1998 Aug 25;37(34):11707-13. PMID:9718293 doi:http://dx.doi.org/10.1021/bi981315i
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