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Fig. 10 | BMC Plant Biology

Fig. 10

From: Protein analysis reveals differential accumulation of late embryogenesis abundant and storage proteins in seeds of wild and cultivated amaranth species

Fig. 10

a, Experimental reported structure for the canonical 11S globulin monomer of A. hypochondriacus (Ah11SA, PDB 3QAC) and structural models generated from 11S globulin paralogs sequences. b, Ah11SB (001411); c, Ah11SPheRich (006768); d, Ah11SHMW (021282). The low RMSD values indicate that all globulins are structural homologues. All globulins present the two β-barrel domains characteristic of these proteins, the highly conserved cysteines are shown in yellow spheres, which are involved in the formation of intra- (IA) and inter-chain (IE) disulphide bonds. The orange region in the model of Ah11SHMW delimits the CTD-like domain exclusive of this paralog, which is not present in any other 11S globulin reported so far

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BMC Plant Biology

ISSN: 1471-2229

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