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Figure 1 | BMC Evolutionary Biology

Figure 1

From: The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands

Figure 1

Structures of representative members of the Bet v 1-like superfamily (A-K) and of oxysterol binding protein (L). A: Birch pollen allergen Bet v 1, Betula verrucosa [PDB:1bv1]; B: STAR-related lipid transport domain of MLN64, Homo sapiens [PDB:1em2]; C: Naphthalene 1,2-dioxygenase, α-chain, C-terminal domain, Pseudomonas putida [PDB:1o7n]; D: Phosphatidylinositol transfer protein alpha, Rattus norvegicus [PDB:1t27]; E: Hypothetical protein NE0264, Nitrosomonas europaea [PDB:1xfs], a member of the AHA1 family; F: Hypothetical protein CC1736, Caulobacter crescentus [PDB:1t17], a member of the polyketide cyclase family; G: Hypothetical protein SMU.440, Streptococcus mutans [PDB:2b79]; H: Hypothetical protein PA1206, Pseudomonas aeruginosa [PDB:2ffs]; I: 2-Oxo-1,2-dihydroquinoline 8-monooxygenase, C-terminal domain, Pseudomonas putida [PDB:1z01], a homotrimeric ring hydroxylase; J: Self-sacrificing resistance protein CalC, Micromonospora echinospora [PDB:1zxf]; K: Hypothetical protein APE2225, Aeropyrum pernix [PDB:2ns9], a member of the CoxG family. L: Oxysterol-binding protein, Saccharomyces cerevisiae [PDB:1zht]. Structures in A-K were coloured according to secondary structure elements homologous to Bet v 1. L was coloured by chain position from blue (N-terminus) to red (C-terminus). Images were generated with UCSF Chimera [61].

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