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ボタンの花色とフラボノイド色素に関する研究

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application/pdf三重大学工学部分子素材工学研究科 分析環境化学研究室48pthesi

(A) Structures of BadA, Hia and YadA heads with the three domains colored according to the domain annotation from the alignment

The superimpositions of the individual domains from all three proteins are shown in the left panel. Note the different order of domains between Hia and BadA. In the BadA Trp-ring domain, 43 of 45 residues could be superimposed to the equivalent Hia domain with an r.m.s.d. of 2.02 Å, and in the GIN domain, 26 of 30 residues could be superimposed with an r.m.s.d. of 1.58 Å. In the BadA neck region, 19 residues could be superimposed to the YadA neck with an r.m.s.d. of 0.28 Å and to the Hia neck with an r.m.s.d. of 1.32 Å. All r.m.s.d. values refer to the C atoms. (B) Sequence alignment of the BadA head with other TAAs. The sequences of Hia and YadA are taken from the published structures; alignments based on these structures were used for homology modeling of the BadA head. The conserved residues that were used to name the domains are marked in bold. Abbreviations used: BhBadA – BadA g