The rumen anaerobic cellulolytic bacterium Eubacterium cellulosolvens produces a large range of cellulases and hemicellulases responsible for the efficient hydrolysis of plant cell wall polysaccharides. One of these enzymes, endoglucanase Cel5A, comprises a tandemly repeated carbohydrate-binding module (CBM65) fused to a glycoside hydrolase family 5 (Cel5A) catalytic domain, joined by flexible linker sequences. The second carbohydrate-binding module located at the C-terminus side of the endoglucanase (CBM65B) has been co-crystallized with either cellohexaose or xyloglucan heptasaccharide. The crystals belong to the hexagonal space group P6(5) and tetragonal space group P4(3)2(1)2, containing a single molecule in the asymmetric unit. The structures of CBM65B have been solved by molecular replacement.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3564627 | PMC |
| http://dx.doi.org/10.1107/S1744309113001620 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Genomic analysis and synergistic effect with cellulase by Streptomyces thermocarboxydus 12219.
Int J Biol Macromol
January 2025
College of Forestry, Henan Agricultural University, Zhengzhou 450046, China. Electronic address:
In this study, we fully sequenced and analyzed the genome of strain 12219 and identified it as Streptomyces thermocarboxydus. The genome contained a single linear chromosome, 6,950,031 bp in size, with a GC content of 72.21 %.
View Article and Find Full Text PDFCharacterization of the CBM50 Gene Family in and Identification of the Putative Effector Gene ThCBM50_1.
J Fungi (Basel)
December 2024
College of Agronomy, Guangxi University, Nanning 530004, China.
Carbohydrate-binding modules (CBMs) are essential virulence factors in phytopathogens, particularly the extensively studied members from the CBM50 gene family, which are known as lysin motif (LysM) effectors and which play crucial roles in plant-pathogen interactions. However, the function of CBM50 in has yet to be fully studied. In this study, we identified seven CBM50 genes from the genome through complete sequence analysis and functional annotation.
View Article and Find Full Text PDFA near-complete telomere-to-telomere genome assembly for Batrachochytrium dendrobatidis GPL JEL423 reveals a larger CBM18 gene family and a smaller M36 metalloprotease gene family than previously recognised.
G3 (Bethesda)
December 2024
MRC Centre for Medical Mycology, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter, United Kingdom, EX4 4QD.
Batrachochytrium dendrobatidis (Bd) is responsible for mass extinctions and extirpations of amphibians, mainly driven by the Global Panzootic Lineage (BdGPL). BdGPL isolate JEL423 is a commonly used reference strain in studies exploring the evolution, epidemiology and pathogenicity of chytrid pathogens. These studies have been hampered by the fragmented, erroneous and incomplete B.
View Article and Find Full Text PDFStructural and functional snapshots of a broad-specificity endoglucanase from Thermogutta terrifontis for biomass saccharification.
Arch Biochem Biophys
December 2024
The Division of Structural Biology, The Nuffield Department of Medicine, University of Oxford, UK; The Rosalind Franklin Institute, Harwell Campus, Didcot, OX11 0QS, UK. Electronic address:
Multifunctionality, processivity, and thermostability are critical for the cost-effective enzymatic saccharification of non-food plant biomass polymers such as β-glucans, celluloses, and xylans to generate biofuels and other valuable products. We present molecular insights into a processive multifunctional endo-1,3-1,4-β-d-glucanase (Tt_End5A) from the hyperthermophilic bacterium Thermogutta terrifontis. Tt_End5A demonstrated activities against a broad spectrum of β-polysaccharides, including barley glucan, lichenan, carboxymethyl cellulose, regenerated amorphous cellulose (RAC), Avicel, xylan, laminarin, mannan, curdlan, xanthan, and various chromogenic substrates at pH 7 and temperatures ranging from 70 to 80°C.
View Article and Find Full Text PDFThe Effect of CBM1 and Linker on the Oxidase, Peroxidase and Monooxygenase Activities of AA9 LPMOs: Insight into Their Correlation with the Nature of Reductants and Crystallinity of Celluloses.
Int J Mol Sci
November 2024
The Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.
This study explores the effect of carbohydrate-binding module 1 (CBM1) and the linker on the function of auxiliary activity 9 (AA9) lytic polysaccharide monooxygenases (LPMOs), with a particular focus on monooxygenase activity, using different crystallinity celluloses and electron donors. The tested C1/C4-oxidizing AA9 LPMOs exhibited higher oxidase and peroxidase activities compared to those of the C4-oxidizing AA9 LPMOs. While the presence of CBM1 promoted cellulose-binding affinity, it reduced the oxidase activity of modular AA9 LPMOs.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!