ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Structure of a fibronectin type III-like module from Clostridium thermocellum.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Role of the CBM11, Fn3, and CBM3 Domains in Enhancing the Multifunctional Enzymatic Activities of Glycoside Hydrolase Family 5 fromJournal of microbiology and biotechnology · 2025Article
- Unique Fn3-like biosensor in σProtein science : a publication of the Protein Society · 2024Article
- A genomic analysis reveals the diversity of cellulosome displaying bacteria.Frontiers in microbiology · 2024Article
- Article
- Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.Current research in microbial sciences · 2021Review
- Functional screening of a Caatinga goat (Capra hircus) rumen metagenomic library reveals a novel GH3 β-xylosidase.PloS one · 2021Article
- Comparative Genomic Analysis Reveals Ecological Differentiation in the GenusFrontiers in microbiology · 2017Article
- The Mechanism by Which Arabinoxylanases Can Recognize Highly Decorated Xylans.The Journal of biological chemistry · 2016Article
- Integration of bacterial lytic polysaccharide monooxygenases into designer cellulosomes promotes enhanced cellulose degradation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Performance of ZDOCK in CAPRI rounds 20-26.Proteins · 2013Article
- Purification, crystallization and preliminary X-ray characterization of the pentamodular arabinoxylanase CtXyl5A from Clostridium thermocellum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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7 authors.
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Abstract
The 1.6 A resolution structure of a fibronectin type III-like module from Clostridium thermocellum (PDB code 3mpc) with two molecules in the asymmetric unit is reported. The crystals used for data collection belonged to space group P2(1)2(1)2(1), with unit-cell parameters a=35.43, b=45.73, c=107.72 A, and the structure was refined to an R factor of 0.166. Structural comparisons found over 800 similar structures in the Protein Data Bank. The broad range of different proteins or protein domains with high structural similarity makes it especially demanding to classify these proteins. Previous studies of fibronectin type III-like modules have indicated that they might function as ligand-binding modules, as a compact form of peptide linkers or spacers between other domains, as cellulose-disrupting modules or as proteins that help large enzyme complexes remain soluble.
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