1987
DOI: 10.1016/0014-5793(87)80130-8
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Predicted structure of tail‐fiber proteins of T‐even type phages

Abstract: The sequences of the tail fiber protein 36 of the phages T 4, T 2, K3, and Ox 2 were analyzed for homologies and for folding patterns using structure prediction methods. No repeating motif was found. A model for the fiber structure is proposed in which fl-strands of about 6 amino acids are separated by turns. In the fl-strand, hydrophobic amino acids are found alternating with hydrophilic ones. Such amphipathic fl-strands can be stabilized by dimer formation. The dimerization occurs in a parallel fashion so th… Show more

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Cited by 10 publications
(6 citation statements)
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“…The annotations of phage homologs vary and include “phage tail tip,” “minor phage tail,” and “putative carbohydrate-binding” proteins. The amino acid sequences of rcc01079 and rcc01080 lack any detectable conserved domains, but predicted secondary structures of both proteins are dominated by β strands, which is consistent with known structures of tail fiber proteins ( Riede et al 1987 ). The observed distribution of rcc01079 and rcc01080 homologs in bacteria and phages implies that these genes are of phage origin and have frequently been horizontally exchanged.…”
Section: Resultssupporting
confidence: 78%
“…The annotations of phage homologs vary and include “phage tail tip,” “minor phage tail,” and “putative carbohydrate-binding” proteins. The amino acid sequences of rcc01079 and rcc01080 lack any detectable conserved domains, but predicted secondary structures of both proteins are dominated by β strands, which is consistent with known structures of tail fiber proteins ( Riede et al 1987 ). The observed distribution of rcc01079 and rcc01080 homologs in bacteria and phages implies that these genes are of phage origin and have frequently been horizontally exchanged.…”
Section: Resultssupporting
confidence: 78%
“…Therefore, it can be speculated that the NS1 region containing the bipartite motif interacts with itself in homo-oligomerization. A similar type of association has previously been reported for a number of homo-oligomeric proteins (51,56,59). Additional experiments particularly with NS1 clones modified by site-directed mutagenesis are needed to assess the role of this putative ␤-strand structure in NS1-NS1 interactions.…”
Section: Discussionsupporting
confidence: 69%
“…Reed et al, proposed a model to predict the three-dimensional structure of t-even phage-type tail fibrin. Their finding were more likely consistent with electron microscopic data [17]. Over computational approach, several models have been developed for phage T7 [13], [18]- [21].…”
Section: Introductionsupporting
confidence: 52%