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Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
TLDR
Striking conformational rearrangements are observed in both the chaperone and target enzyme upon complex formation, and the functionally essential C-terminal domain of yCCS is well positioned to play a key role in the metal ion transfer mechanism.
Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
TLDR
The structures of Hah1 provide models for intermediates in metal ion transfer and suggest a detailed molecular mechanism for protein recognition and metal ion exchange between MT/HCXXC containing domains.
Crystal structure of the copper chaperone for superoxide dismutase
TLDR
The 1.8 Å resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains that are very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake.
The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity.
TLDR
The crystal structure of retinal dehydrogenase type II cocrystallized with nicotinamide adenine dinucleotide (NAD) has been determined and it appears to utilize a disordered loop in the substrate access channel to discriminate between retinaldehyde and short-chain aldehydes.
Crystal structure of the second domain of the human copper chaperone for superoxide dismutase.
TLDR
The X-ray structure of the largest domain of hCCS (hCCS Domain II) is determined and reveals a single loop proximal to the dimer interface which is unique to the CCS chaperones.
Heterodimer formation between superoxide dismutase and its copper chaperone.
TLDR
Heterodimer formation between copper-loaded yCCS and wtSOD1 is accompanied by SOD1 activation only in the presence of zinc, and strongly suggest that in vivo copper loading of yeast S OD1 occurs via a heterodimeric intermediate.
Two Structures of an N-Hydroxylating Flavoprotein Monooxygenase
TLDR
Structural and biochemical evidence indicates that NADP+ remains bound throughout the oxidative half-reaction, which is proposed to shelter the flavin intermediates from solvent and thereby prevent uncoupling of NADPH oxidation from hydroxylated product formation.
Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism.
TLDR
Biochemical comparison of PvdA to p-hydroxybenzoate hydroxylase (PHBH, from Pseudomonas fluorescens) and flavin-containing monooxygenases (FMOs, from Schizosaccharomyces pombe and hog liver microsomes) leads to the hypothesis that Pvd a catalysis proceeds by a novel reaction mechanism.
Staphylopine, pseudopaline, and yersinopine dehydrogenases: A structural and kinetic analysis of a new functional class of opine dehydrogenase
TLDR
The first structural kinetic analyses of enzymes involved in opine metallophore biosynthesis in three important bacterial pathogens of humans are reported, revealing candidate residues in the active sites required for binding of the α-keto acid and nicotianamine-like substrates and for catalysis.
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