2018
DOI: 10.1002/1873-3468.13283
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Function of a laminin_G_3 module as a carbohydrate‐binding module in an arabinofuranosidase from Ruminiclostridium josui

Abstract: Laminin_G_3 modules can exist together with family‐43 catalytic modules of glycoside hydrolase (GH43), but their functions are unknown. Here, a laminin_G_3 module and a GH43 module derived from a Ruminiclostridium josui modular arabinofuranosidase Abf43A‐Abf43B‐Abf43C were produced individually as RjLG3 and RjGH43_22, respectively, or combined as RjGH43‐1 to gain insights into their activities. Isothermal calorimetry analysis showed that RjLG3 has high affinity toward 32‐α‐l‐arabinofuranosyl‐(1,5)‐α‐l‐arabinot… Show more

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Cited by 14 publications
(9 citation statements)
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“…Fast evolution of surface-presented proteins is well-known in pathogens and other bacteria to evade host detection systems and viral attachment sites. Giant ORFs from Omnitrophia frequently encode domains used by eukaryotes for cell adhesion 81,82 . For example, ORFs from Multiplicimicrobium inquinatum (Genome 171) and Omnitrophus fodinae (Genome 190) encode discoidin (PF00754) domains and ORFs from M. inquinatum and SAG-3300015153 (Genome 196) encode laminin_G_3 (PF13385) domains (Supplementary Fig.…”
Section: Genomic Data Suggest Predatory or Parasitic Functionsmentioning
confidence: 99%
“…Fast evolution of surface-presented proteins is well-known in pathogens and other bacteria to evade host detection systems and viral attachment sites. Giant ORFs from Omnitrophia frequently encode domains used by eukaryotes for cell adhesion 81,82 . For example, ORFs from Multiplicimicrobium inquinatum (Genome 171) and Omnitrophus fodinae (Genome 190) encode discoidin (PF00754) domains and ORFs from M. inquinatum and SAG-3300015153 (Genome 196) encode laminin_G_3 (PF13385) domains (Supplementary Fig.…”
Section: Genomic Data Suggest Predatory or Parasitic Functionsmentioning
confidence: 99%
“…Such non-CBM substrate binding modules include "laminin_G_3", "FIVAR", "Big_2", etc., and may alter the affinity or activity of GH catabolic domains with respect to local structural motifs. For example, "laminin_G_3" selectively binds with 3 2 -α-l-arabinofuranosyl-xylobiose and 2 3 ,3 3 -di-α-l-arabinofuranosyl-xylotriose [32],…”
Section: Discussionmentioning
confidence: 99%
“…Such non-CBM substrate binding modules include “laminin_G_3”, “FIVAR”, “Big_2”, etc., and may alter the affinity or activity of GH catabolic domains with respect to local structural motifs. For example, “laminin_G_3” selectively binds with 3 2 -α-l-arabinofuranosyl-xylobiose and 2 3 ,3 3 -di-α-l-arabinofuranosyl-xylotriose [32], suggesting a potential hydrolytic target of branched arabinofuranosyl residues on xylooligomers. “FIVAR” domains have been extensively reported along with CAZymes and are thought to have carbohydrate binding functions, but are not yet well-characterized [33–35].…”
Section: Discussionmentioning
confidence: 99%
“…MC68GH43-1 contains a GH43 domain and a GH43_C domain, while MC72GH43-2 additionally contains a laminin_G_3 domain. A laminin_G_3 domain was reported to play a role in substrate binding of an arabinofuranosidase from Ruminococcus josui , specifically with a branched arabinofuranosyl residue of an arabino-oligosaccharide [ 50 ]. Regarding the exo-arabinofuranosidases, MC72GH43-1 also displayed a multi-modular structure, being composed of a GH43 module and a module associated with some GH43 modules, GH43_C2 (Pfam designation PF17851, beta-xylosidase C-terminal concanavalin A-like domain).…”
Section: Discussionmentioning
confidence: 99%