Cell surface proteins in archaeal and bacterial genomes comprising "LVIVD", "RIVW" and "LGxL" tandem sequence repeats are predicted to fold as beta-propeller.
Proteins that share even low sequence homologies are known to adopt similar folds. The beta-propeller structural motif is one such example. Identifying sequences that adopt a beta-propeller fold is useful to annotate protein structure and function. Often, tandem sequence repeats provide the necessary signal for identifying beta-propellers in proteins. In our recent analysis to identify cell surface proteins in archaeal and bacterial genomes, we identified some proteins that contain novel tandem repeats "LVIVD", "RIVW" and "LGxL". In this work, based on protein fold predictions and three-dimensional comparative modeling methods, we predicted that these repeat types fold as beta-propeller. Further, the evolutionary trace analysis of all proteins constituting amino acid sequence repeats in beta-propellers suggest that the novel repeats have diverged from a common ancestor.
Adindla
Swathi
S
School of Chemistry, University of Hyderabad, Hyderabad 500046, India.
Inampudi
Krishna Kishore
KK
Guruprasad
Lalitha
L
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D016384:Consensus Sequence; D019143:Evolution, Molecular; D020745:Genome, Archaeal; D016680:Genome, Bacterial; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D017020:Methanosarcina / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D020080:Tandem Repeat Sequences
D001426:Bacterial Proteins; D008565:Membrane Proteins