5a29

Family 2 Pectate Lyase from Vibrio vulnificus

spinqualitylabelsall models 5a29, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a29 is a 2 chain structure with sequence from Vibrio vulnificus YJ016. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, MN, SRT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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