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EC Number
Crystallization (Commentary)
apo-enzyme, to 1.39 A resolution, and in complex with NADP+. Enzyme accepts both cofactors NADH and NADPH. Insertions near the N-terminus of the specificity loop probably determine cofactor specificity, the laboratory engineering of NADH preference involved specific loop substitution
in complex with NADH, to 1.54 A resolution. The specificity loop differs significantly from any other crystallized ketol-acid reductoisomerases. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2' hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55
in complex with substrate analog L-tartaric acid, to 2.5 A resolution. The enzyme displays a six-member specificity loop, with residues Arg48 and Ser52 forming hydrogen bonds to the NAD(H) phosphate
to 1.54 A resolution. Structure contains 2 Mg2+ ions and NADH. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2 hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55
Results 1 - 4 of 4