| Title: |
Investigating the spatial configuration of glycoside hydrolase multienzyme complexes on Plant Cell Wall breakdown |
| Authors: |
Montanier, Cédric, Y; Roblin, Pierre; Esque, Jérémy; Ropartz, David; Rogniaux, Hélène; Fanuel, Mathieu; Annic, Bastien; Moraïs, Sarah; Bayer, Edward, A; Dumon, Claire; Pardo Larrabeiti, Iker |
| Contributors: |
Toulouse Biotechnology Institute (TBI); Institut National des Sciences Appliquées - Toulouse (INSA Toulouse); Institut National des Sciences Appliquées (INSA)-Communauté d'universités et établissements de Toulouse (Comue de Toulouse)-Institut National des Sciences Appliquées (INSA)-Communauté d'universités et établissements de Toulouse (Comue de Toulouse)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE); Laboratoire de Génie Chimique (LGC); Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP); Communauté d'universités et établissements de Toulouse (Comue de Toulouse)-Communauté d'universités et établissements de Toulouse (Comue de Toulouse)-Université de Toulouse (EPE UT); Communauté d'universités et établissements de Toulouse (Comue de Toulouse); Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA); Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE); Ben-Gurion University of the Negev (BGU); ANR-21-CE43-0024,Concerto,Control de la proximité spatiale pour des cascades enzymatiques innovantes afin d'améliorer la deconstruction de la biomasse(2021) |
| Source: |
Gordon Research Conference, Carbohydrate-Active Enzymes for Glycan Conversions ; https://hal.inrae.fr/hal-05564028 ; Gordon Research Conference, Carbohydrate-Active Enzymes for Glycan Conversions, Jul 2025, Andover, United States |
| Publisher Information: |
CCSD |
| Publication Year: |
2025 |
| Collection: |
Université Toulouse III - Paul Sabatier: HAL-UPS |
| Subject Terms: |
depolymerases; Jo-In; spatial organization; structure/function characterization; [SDV]Life Sciences [q-bio] |
| Subject Geographic: |
Andover; United States |
| Description: |
International audience ; To address the intricate complexity of plant cell walls (PCWs), anaerobic microorganisms using polysaccharides as carbon source produce an extensive range of glycoside hydrolases (GHs) organized in a multienzymatic complex: the cellulosome. While for the past 15 years, designer cellulosome has been used to study the effect of the spatial arrangement of GHs on enzymatic activities [1;2], the synergies and the spatial position of the different enzymes within the complex are still poorly understood due to its intrinsic flexibility. One approach to address this issue is to lock the spatial proximity between the GHs. To achieve this, we employ the Biomolecular Welding tool (BMW) composed of two small proteins, Jo and In [3]. These proteins spontaneously form an intramolecular isopeptidic bond and offer a unique approach to geometrically freeze the spatial conformation between several GHs [4]. Here, we investigate the correlation between plant cell wall degradation, product profiles, and complex topology using two cellulases (CtCel9R and CtCel8A) and one xylanase (CtXyn11A) from the Clostridium thermocellum cellulosome. |
| Document Type: |
conference object; still image |
| Language: |
English |
| Availability: |
https://hal.inrae.fr/hal-05564028; https://hal.inrae.fr/hal-05564028v1/document; https://hal.inrae.fr/hal-05564028v1/file/Montanier.pdf |
| Rights: |
https://www.etalab.gouv.fr/wp-content/uploads/2017/04/ETALAB-Licence-Ouverte-v2.0.pdf ; info:eu-repo/semantics/OpenAccess |
| Accession Number: |
edsbas.AC2DEF21 |
| Database: |
BASE |