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Prediction of the structural motifs of sandwich proteins.

ABSTRACT: We investigate the supersecondary structure of a large group of proteins, the so-called sandwich proteins. The analysis of a large number of such proteins has led us to propose a set of rules that can be used to predict the possible arrangements of strands in the two beta-sheets forming a given sandwich structure. These rules imply the existence of certain invariant supersecondary substructures common to all sandwich proteins. Furthermore, they dramatically restrict the number of permissible arrangements. For example, whereas for proteins consisting of three strands in each beta-sheet 180 possible strand arrangements exist a priori, our rules imply that only 15 of them are permissible. Five of these predicted arrangements describe all currently known sandwich proteins with six strands.

SUBMITTER: Fokas AS

PROVIDER: S-EPMC534733 | biostudies-literature | 2004 Nov

REPOSITORIES: biostudies-literature

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Prediction of the structural motifs of sandwich proteins.

Fokas A S AS Gelfand I M IM Kister A E AE

Proceedings of the National Academy of Sciences of the United States of America 20041118 48

We investigate the supersecondary structure of a large group of proteins, the so-called sandwich proteins. The analysis of a large number of such proteins has led us to propose a set of rules that can be used to predict the possible arrangements of strands in the two beta-sheets forming a given sandwich structure. These rules imply the existence of certain invariant supersecondary substructures common to all sandwich proteins. Furthermore, they dramatically restrict the number of permissible arr ...[more]

PMID: 15550537

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Project description:BackgroundSeptins are cytoskeletal proteins important in cell division and in establishing and maintaining cell polarity. Although septins are found in various eukaryotes, septin genes had the richest history of duplication and diversification in the animals, fungi and protists that comprise opisthokonts. Opisthokont septin paralogs encode modular proteins that assemble into heteropolymeric higher order structures. The heteropolymers can create physical barriers to diffusion or serve as scaffolds organizing other morphogenetic proteins. How the paralogous septin modules interact to form heteropolymers is still unclear. Through comparative analyses, we hoped to clarify the evolutionary origin of septin diversity and to suggest which amino acid residues were responsible for subunit binding specificity.ResultsHere we take advantage of newly sequenced genomes to reconcile septin gene trees with a species phylogeny from 22 animals, fungi and protists. Our phylogenetic analysis divided 120 septins representing the 22 taxa into seven clades (Groups) of paralogs. Suggesting that septin genes duplicated early in opisthokont evolution, animal and fungal lineages share septin Groups 1A, 4 and possibly also 1B and 2. Group 5 septins were present in fungi but not in animals and whether they were present in the opisthokont ancestor was unclear. Protein homology folding showed that previously identified conserved septin motifs were all located near interface regions between the adjacent septin monomers. We found specific interface residues associated with each septin Group that are candidates for providing subunit binding specificity.ConclusionsThis work reveals that duplication of septin genes began in an ancestral opisthokont more than a billion years ago and continued through the diversification of animals and fungi. Evidence for evolutionary conservation of ~ 49 interface residues will inform mutagenesis experiments and lead to improved understanding of the rules guiding septin heteropolymer formation and from there, to improved understanding of development of form in animals and fungi.

Dataset Information

Prediction of the structural motifs of sandwich proteins.

Publications

Prediction of the structural motifs of sandwich proteins.

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