Abstract

<p>A) The AldA tetramer is shown as a ribbon tracing with each subunit differentially colored. Two subunits (gold and white) were in the asymmetric unit of the crystal with the other two subunits (green and rose) related by crystallographic symmetry. N-termini are labeled. B) Domain organization of the AldA monomer. The view is rotated 90° relative to panel A and shows the two subunits in the asymmetric unit. The catalytic (red), cofactor binding (blue), and oligomerization (rose) domains are highlighted in one monomer. The position of NAD<sup>+</sup> (space-filling model) is indicated. C) Substrate binding sites on opposite sides of the AldA monomer. The two views of an AldA monomer are rotated 180° and show the locations of the NAD(H) and IAAld/IAA binding sites on each face of the monomer. D) Ligand binding tunnel. The positions of NAD<sup>+</sup> (rose) and IAA (gold) in the tunnel (grey surface) relative to the catalytic cysteine (Cys302) are shown. The position of docked IAAld (rose), which overlaps with IAA, is indicated.</p

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