|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='5a8o' size='340' side='right'caption='[[5a8o]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5a8o' size='340' side='right'caption='[[5a8o]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a8o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Microbulbifer_degradans_2-40 Microbulbifer degradans 2-40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A8O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a8o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharophagus_degradans_2-40 Saccharophagus degradans 2-40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A8O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CTT:BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSE'>CTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a8m|5a8m]], [[5a8n|5a8n]], [[5a8p|5a8p]], [[5a8q|5a8q]], [[5a94|5a94]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] </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=5a8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8o OCA], [https://pdbe.org/5a8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a8o RCSB], [https://www.ebi.ac.uk/pdbsum/5a8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8o ProSAT]</span></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=5a8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8o OCA], [http://pdbe.org/5a8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a8o RCSB], [http://www.ebi.ac.uk/pdbsum/5a8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q21KE5_SACD2 Q21KE5_SACD2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5a8o" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5a8o" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 23: |
Line 27: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Licheninase]] | + | [[Category: Saccharophagus degradans 2-40]] |
| - | [[Category: Microbulbifer degradans 2-40]]
| + | [[Category: Berrin JG]] |
| - | [[Category: Berrin, J G]] | + | [[Category: Coutinho RM]] |
| - | [[Category: Coutinho, R M]] | + | [[Category: Freyd T]] |
| - | [[Category: Freyd, T]] | + | [[Category: Garron ML]] |
| - | [[Category: Garron, M L]] | + | [[Category: Henrissat B]] |
| - | [[Category: Henrissat, B]] | + | [[Category: Lafond M]] |
| - | [[Category: Lafond, M]] | + | [[Category: Sulzenbacher G]] |
| - | [[Category: Sulzenbacher, G]] | + | |
| - | [[Category: Beta-glucanase]]
| + | |
| - | [[Category: Cazyme]]
| + | |
| - | [[Category: Gh5_26]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
5a8o is a 1 chain structure with sequence from Saccharophagus degradans 2-40. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q21KE5_SACD2
Publication Abstract from PubMed
In the CAZy database, glycoside hydrolase family 5 (GH5) is a large family with more than 6,000 sequences. Among the 51 described GH5 subfamilies, subfamily GH5_26 contains members that display either endo- beta(1,4)-glucanase or beta(1,3;1,4)-glucanase activities. In this study, we focused on the GH5_26 enzyme from Saccharophagus degradans (SdGluc5_26A) a marine bacterium known for its capacity to degrade a wide diversity of complex polysaccharides. SdGluc5_26A displays lichenase activity towards beta(1,3;1,4)-glucans with a side cellobiohydrolase activity towards beta(1,4)-glucans. The 3D structure of SdGluc5_26A adopts a stable trimeric quaternary structure observable also in solution. The N-terminal region of SdGluc5_26A protrudes into the active site of an adjacent monomer. To understand whether this occupation of the active site could influence its activity, we conducted a comprehensive enzymatic characterization of SdGluc5_26A and of a mutant truncated at the N-terminus. Ligand complex structures and kinetic analyses reveal that the N-terminus governs the substrate specificity of SdGluc5_26A. Its deletion opens the enzyme cleft at the -3 subsite and turns the enzyme into an endo-beta(1,4)-glucanase. This study demonstrates that experimental approaches can reveal structure-function relationships out of reach of current bioinformatic predictions.
the quaternary structure of a glycoside hydrolase dictates specificity towards beta-glucans.,Lafond M, Sulzenbacher G, Freyd T, Henrissat B, Berrin JG, Garron ML J Biol Chem. 2016 Jan 11. pii: jbc.M115.695999. PMID:26755730[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lafond M, Sulzenbacher G, Freyd T, Henrissat B, Berrin JG, Garron ML. the quaternary structure of a glycoside hydrolase dictates specificity towards beta-glucans. J Biol Chem. 2016 Jan 11. pii: jbc.M115.695999. PMID:26755730 doi:http://dx.doi.org/10.1074/jbc.M115.695999
|
