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September 2023 issue
Cover illustration: Crystal structure of NADPH-dependent imine reductase from Ajellomyces dermatitidis [Sharma et al. (2023), Acta Cryst. F79, 224–230], which catalyzes the reductive amination of certain ketones with amine donorss. This structure belongs to space group P3121 and features two molecules in the asymmetric unit complexed with NADPH4.
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The structure of the imine reductase from A. dermatitidis is presented in three crystal forms, each of which provides information on conformational dynamics and cofactor and substrate binding within the enzyme.
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Colchicalin is an engineered binding protein derived from the lipocalin scaffold, which provides a binding site comprised of four loops exhibiting structural plasticity. Structural analysis of this lipocalin in the absence and the presence of its ligand colchicine reveals drastic structural changes which indicate a conformational selection mechanism.
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The crystal structure of the Mu8.1 conotoxin was determined in the high-symmetry space group I4122 at 1.67 Å resolution. This crystal structure reveals a surface-exposed Zn2+-binding site and establishes a hydrogen-bonding network around Lys55 buried at the dimer interface.
PDB reference: Mu8.1, 8amy
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