The CATH classification revisited—architectures reviewed and new ways to characterize structural divergence in superfamilies

The latest version of CATH (class, architecture, topology, homology) (version 3.2), released in July 2008 (http://www.cathdb.info), contains 1 14 215 domains, 2178 Homologous superfamilies and 1110 fold groups. We have assigned 20 330 new domains, 87 new homologous superfamilies and 26 new folds since CATH release version 3.1. A total of 28 064 new domains have been assigned since our NAR 2007 database publication (CATH version 3.0). The CATH website has been completely redesigned and includes more comprehensive documentation. We have revisited the CATH architecture level as part of the development of a ‘Protein Chart’ and present information on the population of each architecture. The CATHEDRAL structure comparison algorithm has been improved and used to characterize structural diversity in CATH superfamilies and structural overlaps between superfamilies. Although the majority of superfamilies in CATH are not structurally diverse and do not overlap significantly with other superfamilies, ∼4% of superfamilies are very diverse and these are the superfamilies that are most highly populated in both the PDB and in the genomes. Information on the degree of structural diversity in each superfamily and structural overlaps between superfamilies can now be downloaded from the CATH website.

[1]  N. Grishin Fold change in evolution of protein structures. , 2001, Journal of structural biology.

[2]  I. Polikarpov,et al.  Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose. , 2004, Journal of molecular biology.

[3]  K. Diederichs,et al.  Structural Basis of Light Harvesting by Carotenoids: Peridinin-Chlorophyll-Protein from Amphidinium carterae , 1996, Science.

[4]  S. Steinbacher,et al.  Crystal structure and mechanism of human L‐arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis , 1998, The EMBO journal.

[5]  William R. Taylor,et al.  A ‘periodic table’ for protein structures , 2002, Nature.

[6]  D. T. Jones,et al.  Beta propellers: structural rigidity and functional diversity. , 1999, Current opinion in structural biology.

[7]  Alan R Davidson,et al.  A folding space odyssey , 2008, Proceedings of the National Academy of Sciences.

[8]  D Eisenberg,et al.  Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. , 1997, Science.

[9]  R. Kolodny,et al.  Protein structure comparison: implications for the nature of 'fold space', and structure and function prediction. , 2006, Current opinion in structural biology.

[10]  Satish K Nair,et al.  Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters. , 2007, Structure.

[11]  Markus Gruber,et al.  A discrete view on fold space , 2008, Bioinform..

[12]  David T. Jones,et al.  β Propellers: structural rigidity and functional diversity , 1999 .

[13]  David C. Jones,et al.  CATH--a hierarchic classification of protein domain structures. , 1997, Structure.

[14]  Eric Martz The Protein Chart , 2010 .

[15]  Frances M. G. Pearl,et al.  CATHEDRAL: A Fast and Effective Algorithm to Predict Folds and Domain Boundaries from Multidomain Protein Structures , 2007, PLoS Comput. Biol..

[16]  Gabrielle A. Reeves,et al.  Structural diversity of domain superfamilies in the CATH database. , 2006, Journal of molecular biology.

[17]  A Wlodawer,et al.  Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology. , 2000, Structure.

[18]  Nigel J. Martin,et al.  Gene3D: comprehensive structural and functional annotation of genomes , 2007, Nucleic Acids Res..

[19]  Christine A. Orengo,et al.  The Protein Chart , 2008 .

[20]  Frances M. G. Pearl,et al.  The CATH domain structure database: new protocols and classification levels give a more comprehensive resource for exploring evolution , 2006, Nucleic Acids Res..

[21]  Nick V. Grishin,et al.  Structural drift: a possible path to protein fold change , 2005, Bioinform..