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Figure 2
Overall structural analysis of AtGSA1. (a) Stereoview of dimeric AtGSA1 in cartoon representation with cofactors depicted in stick representation. The N-terminal domain, cofactor-binding domain and C-terminal domain are shown in green, cyan and salmon, respectively. The gating-loop region (residues 151–184) is shown in magenta. (b) Comparison of subunit A and subunit B. (c) Multiple sequence alignment of GSAM from A. thaliana (AtGSA1, sequence without transit peptide), Synechococcus elongatus, B. subtilis, Y. pestis, T. thermophilus and Aeropyrum pernix. The secondary structure of AtGSA1 is displayed above the sequences. Identical amino acids are in white on a red background. The similar residues are in red and boxed. Dots indicate gaps introduced during alignment. Blue circles denote the residues involved in negative cooperativity. Magenta circles denote the residues involved in gating-loop reorientation.

ISSN: 2053-230X
Volume 72| Part 6| June 2016| Pages 448-456
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