Figure 2 | Scientific Reports

Figure 2

From: Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD+ Binding and the Cofactor Positioned to Accept a Hydride

Figure 2

Sequence alignment of HDH enzymes from various sources: MtHDH, Medicago truncatula [UniProt accession number: G7IKX3]; AtHDH, Arabidopsis thaliana [Q9C5U8-1]; BoHDH, Brassica oleracea [P24226]; EcHisD, Escherichia coli (strain K12) [P06988]; MtHisD, Mycobacterium tuberculosis (strain H37Rv) [P9WNW9]; StHisD, Salmonella typhimurium (strain LT2) [P10370]; BsHisD, Brucella suis biovar 1 (strain 1330) [Q8G2R2]. For clarity of the alignment, the N-terminal signal peptides of At and Bo enzymes were truncated at positions 31 and 32, respectively, which correspond to Pro42 in Mt structure, which is the first residue visible in the electron density. Domains of MtHDH are coloured: I, orange; II, magenta; III, turquoise; IV, chartreuse. Elements of the secondary structure are: α-helices, yellow; 310 helices, red; β-strands, cyan. Helices are numbered consecutively, regardless of the type.

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