Literature DB >> 15095989

Supra-domains: evolutionary units larger than single protein domains.

Christine Vogel1, Carlo Berzuini, Matthew Bashton, Julian Gough, Sarah A Teichmann.   

Abstract

Domains are the evolutionary units that comprise proteins, and most proteins are built from more than one domain. Domains can be shuffled by recombination to create proteins with new arrangements of domains. Using structural domain assignments, we examined the combinations of domains in the proteins of 131 completely sequenced organisms. We found two-domain and three-domain combinations that recur in different protein contexts with different partner domains. The domains within these combinations have a particular functional and spatial relationship. These units are larger than individual domains and we term them "supra-domains". Amongst the supra-domains, we identified some 1400 (1203 two-domain and 166 three-domain) combinations that are statistically significantly over-represented relative to the occurrence and versatility of the individual component domains. Over one-third of all structurally assigned multi-domain proteins contain these over-represented supra-domains. This means that investigation of the structural and functional relationships of the domains forming these popular combinations would be particularly useful for an understanding of multi-domain protein function and evolution as well as for genome annotation. These and other supra-domains were analysed for their versatility, duplication, their distribution across the three kingdoms of life and their functional classes. By examining the three-dimensional structures of several examples of supra-domains in different biological processes, we identify two basic types of spatial relationships between the component domains: the combined function of the two domains is such that either the geometry of the two domains is crucial and there is a tight constraint on the interface, or the precise orientation of the domains is less important and they are spatially separate. Frequently, the role of the supra-domain becomes clear only once the three-dimensional structure is known. Since this is the case for only a quarter of the supra-domains, we provide a list of the most important unknown supra-domains as potential targets for structural genomics projects.

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Year:  2004        PMID: 15095989     DOI: 10.1016/j.jmb.2003.12.026

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  63 in total

Review 1.  The interface of protein structure, protein biophysics, and molecular evolution.

Authors:  David A Liberles; Sarah A Teichmann; Ivet Bahar; Ugo Bastolla; Jesse Bloom; Erich Bornberg-Bauer; Lucy J Colwell; A P Jason de Koning; Nikolay V Dokholyan; Julian Echave; Arne Elofsson; Dietlind L Gerloff; Richard A Goldstein; Johan A Grahnen; Mark T Holder; Clemens Lakner; Nicholas Lartillot; Simon C Lovell; Gavin Naylor; Tina Perica; David D Pollock; Tal Pupko; Lynne Regan; Andrew Roger; Nimrod Rubinstein; Eugene Shakhnovich; Kimmen Sjölander; Shamil Sunyaev; Ashley I Teufel; Jeffrey L Thorne; Joseph W Thornton; Daniel M Weinreich; Simon Whelan
Journal:  Protein Sci       Date:  2012-04-23       Impact factor: 6.725

2.  Fine-tuning of protein domain boundary by minimizing potential coiled coil regions.

Authors:  Naoko Iwaya; Natsuko Goda; Satoru Unzai; Kenichiro Fujiwara; Toshiki Tanaka; Kentaro Tomii; Hidehito Tochio; Masahiro Shirakawa; Hidekazu Hiroaki
Journal:  J Biomol NMR       Date:  2006-12-16       Impact factor: 2.835

3.  Reductive evolution of architectural repertoires in proteomes and the birth of the tripartite world.

Authors:  Minglei Wang; Liudmila S Yafremava; Derek Caetano-Anollés; Jay E Mittenthal; Gustavo Caetano-Anollés
Journal:  Genome Res       Date:  2007-10-01       Impact factor: 9.043

Review 4.  Exploiting protein structure data to explore the evolution of protein function and biological complexity.

Authors:  Russell L Marsden; Juan A G Ranea; Antonio Sillero; Oliver Redfern; Corin Yeats; Michael Maibaum; David Lee; Sarah Addou; Gabrielle A Reeves; Timothy J Dallman; Christine A Orengo
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2006-03-29       Impact factor: 6.237

Review 5.  Nothing about protein structure classification makes sense except in the light of evolution.

Authors:  Ruben E Valas; Song Yang; Philip E Bourne
Journal:  Curr Opin Struct Biol       Date:  2009-04-24       Impact factor: 6.809

6.  Structure prediction of domain insertion proteins from structures of individual domains.

Authors:  Monica Berrondo; Marc Ostermeier; Jeffrey J Gray
Journal:  Structure       Date:  2008-04       Impact factor: 5.006

7.  Consequences of domain insertion on sequence-structure divergence in a superfold.

Authors:  Chetanya Pandya; Shoshana Brown; Ursula Pieper; Andrej Sali; Debra Dunaway-Mariano; Patricia C Babbitt; Yu Xia; Karen N Allen
Journal:  Proc Natl Acad Sci U S A       Date:  2013-08-19       Impact factor: 11.205

8.  Nature of the protein universe.

Authors:  Michael Levitt
Journal:  Proc Natl Acad Sci U S A       Date:  2009-06-18       Impact factor: 11.205

9.  Comparative evolutionary analysis of protein complexes in E. coli and yeast.

Authors:  Adam J Reid; Juan Ag Ranea; Christine A Orengo
Journal:  BMC Genomics       Date:  2010-02-01       Impact factor: 3.969

10.  Development of an accurate classification system of proteins into structured and unstructured regions that uncovers novel structural domains: its application to human transcription factors.

Authors:  Satoshi Fukuchi; Keiichi Homma; Yoshiaki Minezaki; Takashi Gojobori; Ken Nishikawa
Journal:  BMC Struct Biol       Date:  2009-04-30
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