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| | <StructureSection load='7o77' size='340' side='right'caption='[[7o77]], [[Resolution|resolution]] 2.32Å' scene=''> | | <StructureSection load='7o77' size='340' side='right'caption='[[7o77]], [[Resolution|resolution]] 2.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7o77]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Psea6 Psea6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O77 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7o77]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_atlantica_T6c Pseudoalteromonas atlantica T6c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O77 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.321Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Patl_3640 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=342610 PSEA6])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Poly(beta-D-mannuronate)_lyase Poly(beta-D-mannuronate) lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.3 4.2.2.3] </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=7o77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o77 OCA], [https://pdbe.org/7o77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o77 RCSB], [https://www.ebi.ac.uk/pdbsum/7o77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o77 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=7o77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o77 OCA], [https://pdbe.org/7o77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o77 RCSB], [https://www.ebi.ac.uk/pdbsum/7o77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o77 ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psea6]] | + | [[Category: Pseudoalteromonas atlantica T6c]] |
| - | [[Category: Aghajari, N]] | + | [[Category: Aghajari N]] |
| - | [[Category: Ballut, L]] | + | [[Category: Ballut L]] |
| - | [[Category: Carrique, L]] | + | [[Category: Carrique L]] |
| - | [[Category: Violot, S]] | + | [[Category: Violot S]] |
| - | [[Category: Beta helix]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The Polysaccharide Lyase Family 6 (PL6) represents one of the 41 polysaccharide lyase families classified in the CAZy database with the vast majority of its members being alginate lyases grouped into three subfamilies, PL6_1-3. To decipher the mode of recognition and action of the enzymes belonging to subfamily PL6_1, we solved the crystal structures of Pedsa0632, Patl3640, Pedsa3628 and Pedsa3807, which all show different substrate specificities and mode of action (endo-/exo-lyase). Thorough exploration of the structures of Pedsa0632 and Patl3640 in complex with their substrates as well as docking experiments confirm that the conserved residues in subsites -1 to +3 of the catalytic site form a common platform which can accommodate various types of alginate in a very similar manner but with a series of original adaptations bringing them their specificities of action. From comparative studies with existing structures of PL6_1 alginate lyases, we observe that in the right-handed parallel beta-helix fold shared by all these enzymes, the substrate binding site harbors the same overall conserved structures and organization. Despite this apparent similarity, it appears that members of the PL6_1 subfamily specifically accommodate and catalyze the degradation of different alginates suggesting that this common platform is actually a highly adaptable and specific tool.
Exploring molecular determinants of polysaccharide Lyase family 6-1 enzyme activity.,Violot S, Galisson F, Carrique L, Jugnarain V, Conchou L, Robert X, Thureau A, Helbert W, Aghajari N, Ballut L Glycobiology. 2021 Jul 10. pii: 6318796. doi: 10.1093/glycob/cwab073. PMID:34245266[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Violot S, Galisson F, Carrique L, Jugnarain V, Conchou L, Robert X, Thureau A, Helbert W, Aghajari N, Ballut L. Exploring molecular determinants of polysaccharide Lyase family 6-1 enzyme activity. Glycobiology. 2021 Jul 10. pii: 6318796. doi: 10.1093/glycob/cwab073. PMID:34245266 doi:http://dx.doi.org/10.1093/glycob/cwab073
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