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| | <StructureSection load='6itg' size='340' side='right'caption='[[6itg]], [[Resolution|resolution]] 1.42Å' scene=''> | | <StructureSection load='6itg' size='340' side='right'caption='[[6itg]], [[Resolution|resolution]] 1.42Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6itg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"photobacter_splendidum"_(sic)_beijerinck_1900 "photobacter splendidum" (sic) beijerinck 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ITG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ITG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6itg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_splendidus Vibrio splendidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ITG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ITG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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]] 1.42Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BTO12_02510 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29497 "Photobacter splendidum" (sic) Beijerinck 1900])</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>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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=6itg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6itg OCA], [http://pdbe.org/6itg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6itg RCSB], [http://www.ebi.ac.uk/pdbsum/6itg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6itg 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=6itg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6itg OCA], [https://pdbe.org/6itg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6itg RCSB], [https://www.ebi.ac.uk/pdbsum/6itg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6itg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A2S7V3I3_VIBSP A0A2S7V3I3_VIBSP] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, W Z]] | + | [[Category: Vibrio splendidus]] |
| - | [[Category: Lyu, Q Q]] | + | [[Category: Liu WZ]] |
| - | [[Category: Lyase]] | + | [[Category: Lyu QQ]] |
| Structural highlights
Function
A0A2S7V3I3_VIBSP
Publication Abstract from PubMed
Alginate lyases have a wide range of industrial applications, such as oligosaccharide preparation, medical treatment, and bioconversion. Therefore, the discovery and characterization of novel alginate lyases are extremely important. PL-6 alginate lyases are classified into two groups: those with a single domain or two domains. However, only one structure of a two-domain alginate lyase has been determined to date. In this study, we characterized a novel single-domain PL-6 alginate lyase (named AlyF). According to the biochemical analysis, AlyF possesses unique features compared with other PL-6 enzymes, including (1) a Ca(2+)-independent catalytic mechanism and (2) a PolyG-specific cleavage specificity that predominantly produces trisaccharides. The structures of AlyF and its complexes described here reveal the structural basis for these unique features and substrate binding mechanisms, which were further confirmed using mutagenesis. More importantly, we determined the possible subsites specifying the predominantly trisaccharide products of AlyF, which may facilitate the rational design of AlyF for potential applications in preparing a single alginate oligomer.
Structural insights into a novel Ca(2+)-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution.,Lyu Q, Zhang K, Shi Y, Li W, Diao X, Liu W Biochim Biophys Acta Gen Subj. 2019 Apr 17;1863(7):1167-1176. doi:, 10.1016/j.bbagen.2019.04.013. PMID:31004719[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lyu Q, Zhang K, Shi Y, Li W, Diao X, Liu W. Structural insights into a novel Ca(2+)-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution. Biochim Biophys Acta Gen Subj. 2019 Apr 17;1863(7):1167-1176. doi:, 10.1016/j.bbagen.2019.04.013. PMID:31004719 doi:http://dx.doi.org/10.1016/j.bbagen.2019.04.013
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