4EYZ

Crystal structure of an uncommon cellulosome-related protein module from Ruminococcus flavefaciens that resembles papain-like cysteine peptidases

Summary for 4EYZ

• Entry DOI: 10.2210/pdb4eyz/pdb
• Descriptor: Cellulosome-related protein module from Ruminococcus flavefaciens that resembles papain-like cysteine peptidases, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: putative protease, hydrolase
• Biological source: Ruminococcus flavefaciens
• Total number of polymer chains: 2
• Total formula weight: 55054.82

Authors

Frolow, F.,Voronov-Goldman, M.,Bayer, E.,Lamed, R. (deposition date: 2012-05-02, release date: 2013-03-20, Last modification date: 2025-03-26)

Primary citation

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.
Crystal Structure of an Uncommon Cellulosome-Related Protein Module from Ruminococcus flavefaciens That Resembles Papain-Like Cysteine Peptidases.
Plos One, 8:e56138-e56138, 2013

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.

PubMed: 23457513
DOI: 10.1371/journal.pone.0056138

Experimental method

X-RAY DIFFRACTION (1.383 Å)