Structural constraints and emergence of sequence patterns in protein evolution.
The aim of this work was to study the relationship between structure conservation and sequence divergence in protein evolution. To this end, we developed a model of structurally constrained protein evolution (SCPE) in which trial sequences, generated by random mutations at gene level, are selected against departure from a reference three-dimensional structure. Since at the mutational level SCPE is completely unbiased, any emergent sequence pattern will be due exclusively to structural constraints. In this first report, it is shown that SCPE correctly predicts the characteristic hexapeptide motif of the left-handed parallel beta helix (LbetaH) domain of UDP-N-acetylglucosamine acyltransferases (LpxA).
Parisi
G
G
Universidad Nacional de Quilmes, Bernal, Argentina.
Echave
J
J
D000217:Acyltransferases / Q000737:chemistry; D000595:Amino Acid Sequence / Q000235:genetics; D003198:Computer Simulation; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics*; D019143:Evolution, Molecular; D008962:Models, Theoretical; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary / Q000235:genetics*; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D013379:Substrate Specificity / Q000235:genetics
D011506:Proteins; D000217:Acyltransferases; C050304:acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferase