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| | <StructureSection load='5a29' size='340' side='right'caption='[[5a29]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5a29' size='340' side='right'caption='[[5a29]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_vulnificus Vibrio vulnificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A29 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a29]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_vulnificus_YJ016 Vibrio vulnificus YJ016]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A29 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</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=5a29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a29 OCA], [http://pdbe.org/5a29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a29 RCSB], [http://www.ebi.ac.uk/pdbsum/5a29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a29 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=5a29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a29 OCA], [https://pdbe.org/5a29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a29 RCSB], [https://www.ebi.ac.uk/pdbsum/5a29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a29 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7MCK3_VIBVY Q7MCK3_VIBVY] |
| | <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: Vibrio vulnificus]] | + | [[Category: Vibrio vulnificus YJ016]] |
| - | [[Category: Abbott, D W]] | + | [[Category: Abbott DW]] |
| - | [[Category: Boraston, A B]] | + | [[Category: Boraston AB]] |
| - | [[Category: Hobbs, J K]] | + | [[Category: Hobbs JK]] |
| - | [[Category: Jones, D]] | + | [[Category: Jones D]] |
| - | [[Category: McLean, R]] | + | [[Category: McLean R]] |
| - | [[Category: Suits, M D]] | + | [[Category: Suits MD]] |
| - | [[Category: Tuomivaara, S]] | + | [[Category: Tuomivaara S]] |
| - | [[Category: Ancestral gene resurrection]]
| + | |
| - | [[Category: Beta-elimination]]
| + | |
| - | [[Category: Endolytic]]
| + | |
| - | [[Category: Exolytic]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Magnesium]]
| + | |
| - | [[Category: Pectin]]
| + | |
| - | [[Category: Polysaccharide lyase]]
| + | |
| Structural highlights
Function
Q7MCK3_VIBVY
Publication Abstract from PubMed
Family 2 polysaccharide lyases (PL2s) preferentially catalyze the beta-elimination of homogalacturonan (HG) using transition metals as catalytic cofactors. PL2 is divided into two subfamilies that have been generally associated with secretion, Mg2+-dependence, and endolysis (subfamily 1); and intracellular localization, Mn2+-dependence, and exolysis (subfamily 2). When present within a genome, PL2s are typically found as tandem copies, which suggest that they provide complementary activities at different stages along a catabolic cascade. This relationship most likely evolved by gene duplication and neofunctionalization. Although the molecular basis of subfamily 1 endolytic activity is understood, the adaptations within the active site of subfamily 2 enzymes that contribute to exolysis have not been determined. In order to investigate this process, we have conducted a comparative enzymatic analysis of enzymes dispersed within the PL2 phylogenetic tree, and elucidated the structure of VvPL2 from Vibrio vulnificus YJ016, which represents a transitional member between subfamiles 1 and 2. In addition, we have used ancestral sequence reconstruction (ASR) to functionally investigate the segregated evolutionary history of PL2 progenitor enzymes and illuminate the molecular evolution of exolysis. This study highlights that ASR in combination with the comparative analysis of contemporary and resurrected enzymes holds promise for elucidating the origins and activities of other carbohydrate active enzyme families and the biological significance of cryptic metabolic pathways, such as pectinolysis within the zoonotic marine pathogen V. vulnificus.
Functional analyses of resurrected and contemporary enzymes illuminate an evolutionary path for the emergence of exolysis in polysaccharide lyase family two.,McLean R, Hobbs JK, Suits MD, Tuomivaara ST, Jones D, Boraston AB, Abbott DW J Biol Chem. 2015 Jul 9. pii: jbc.M115.664847. PMID:26160170[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McLean R, Hobbs JK, Suits MD, Tuomivaara ST, Jones D, Boraston AB, Abbott DW. Functional analyses of resurrected and contemporary enzymes illuminate an evolutionary path for the emergence of exolysis in polysaccharide lyase family two. J Biol Chem. 2015 Jul 9. pii: jbc.M115.664847. PMID:26160170 doi:http://dx.doi.org/10.1074/jbc.M115.664847
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