Crystal Structure of an Uncommon Cellulosome-Related Protein Module from Ruminococcus flavefaciens That Resembles Papain-Like Cysteine Peptidases.
Levy-Assaraf, M., Voronov-Goldman, M., Rozman Grinberg, I., Weiserman, G., Shimon, L.J., Jindou, S., Borovok, I., White, B.A., Bayer, E.A., Lamed, R., Frolow, F.(2013) PLoS One 8: e56138-e56138
- PubMed: 23457513 
- DOI: https://doi.org/10.1371/journal.pone.0056138
- Primary Citation of Related Structures:  
4EYZ - PubMed Abstract: 
Ruminococcus flavefaciens is one of the predominant fiber-degrading bacteria found in the rumen of herbivores. Bioinformatic analysis of the recently sequenced genome indicated that this bacterium produces one of the most intricate cellulosome systems known to date. A distinct ORF, encoding for a multi-modular protein, RflaF_05439, was discovered during mining of the genome sequence. It is composed of two tandem modules of currently undefined function that share 45% identity and a C-terminal X-dockerin modular dyad. Gaining insight into the diversity, architecture and organization of different types of proteins in the cellulosome system is essential for broadening our understanding of a multi-enzyme complex, considered to be one of the most efficient systems for plant cell wall polysaccharide degradation in nature.
Organizational Affiliation: 
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv, Israel.