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Figure 1.
Crystal structure of GSAM in the PMP (KE-4)/PLP (DAVA-IA)
form. (A) Overall stereo presentation of α2-dimeric GSAM. In
subunit A, the N- and C-terminal domains as well as the cofactor
binding domain are shown in different blue tones. Subunit B is
shown in yellow. Cofactors and catalytic intermediates are
highlighted. Both termini are denoted. The gating-loop regions
disobeying local 2-fold symmetry and the interface helices
(residues 121–138) are shown in blue (open) and red (closed),
respectively. The gating loop is located at the dimer interface
and extends toward the active site in the closed conformation.
(B) Superposition of residues 150–183 in open (light
blue/blue) and closed (yellow/red) conformation. Cofactors
within the active sites are colored accordingly. The hinge
element (Leu-158 and Ser-172) and Ser-163 are denoted. The
β-hydroxy group of Ser-163 moves ≈22 Å.
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