Accounting for solvent accessibility and secondary structure in protein phylogenetics is clearly beneficial.
Amino acid substitution models are essential to most methods to infer phylogenies from protein data. These models represent the ways in which proteins evolve and substitutions accumulate along the course of time. It is widely accepted that the substitution processes vary depending on the structural configuration of the protein residues. However, this information is very rarely used in phylogenetic studies, though the 3-dimensional structure of dozens of thousands of proteins has been elucidated. Here, we reinvestigate the question in order to fill this gap. We use an improved estimation methodology and a very large database comprising 1471 nonredundant globular protein alignments with structural annotations to estimate new amino acid substitution models accounting for the secondary structure and solvent accessibility of the residues. These models incorporate a confidence coefficient that is estimated from the data and reflects the reliability and usefulness of structural annotations in the analyzed sequences. Our results with 300 independent test alignments show an impressive likelihood gain compared with standard models such as JTT or WAG. Moreover, the use of these models induces significant topological changes in the inferred trees, which should be of primary interest to phylogeneticists. Our data, models, and software are available for download from http://atgc.lirmm.fr/phyml-structure/.
Méthodes et Algorithmes pour la Bioinformatique, LIRMM, CNRS-Université Montpellier II, 161 rue Ada, Montpellier Cedex 5, France.
Si Quang
SQ
Le
Olivier
O
Gascuel
D000595:Amino Acid Sequence; D002965:Classification / Q000379:methods*; D030541:Databases, Genetic; D019143:Evolution, Molecular; D016013:Likelihood Functions; D008957:Models, Genetic; D010802:Phylogeny; D011487:Protein Conformation; D011506:Proteins / Q000235:genetics*; D016415:Sequence Alignment; D012984:Software
D011506:Proteins