ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Structure of CBM4 from Clostridium thermocellum cellulase K.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- The In Silico Characterization of Monocotyledonous α-l-Arabinofuranosidases on the Example of Maize.Life (Basel, Switzerland) · 2023Article
- Review
- Multimodularity of a GH10 Xylanase Found in the Termite Gut Metagenome.Applied and environmental microbiology · 2021Article
- A metagenome-derived thermostable β-glucanase with an unusual module architecture which defines the new glycoside hydrolase family GH148.Scientific reports · 2017Article
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5 authors.
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Abstract
Here, a 2.0 Å resolution X-ray structure of Clostridium thermocellum cellulase K family 4 carbohydrate-binding module (CelK CBM4) is reported. The resulting structure was refined to an R factor of 0.212 and an R(free) of 0.274. Structural analysis shows that this new structure is very similar to the previously solved structure of C. thermocellum CbhA CBM4. Most importantly, these data support the previously proposed notion of an extended binding pocket using a novel tryptophan-containing loop that may be highly conserved in clostridial CBM4 proteins.
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