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The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites
Protein disulfide isomerase plays a key role in catalyzing the folding of secretory proteins. It features two catalytically inactive thioredoxin domains inserted between two catalytically active… Expand
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB–MoaD complex
The activation of ubiquitin and related protein modifiers is catalysed by members of the E1 enzyme family that use ATP for the covalent self-attachment of the modifiers to a conserved cysteine. The… Expand
Structural Insights into E1-Catalyzed Ubiquitin Activation and Transfer to Conjugating Enzymes
Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific cascades involving three classes of enzymes, E1, E2, and E3. Each E1 adenylates the C terminus of its… Expand
Molecular Basis of Sulfite Oxidase Deficiency from the Structure of Sulfite Oxidase
The molybdenum-containing enzyme sulfite oxidase catalyzes the conversion of sulfite to sulfate, the terminal step in the oxidative degradation of cysteine and methionine. Deficiency of this enzyme… Expand
Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
THE cold-shock response in both Escherichia coli and Bacillus subtilis is induced by an abrupt downshift in growth temperature. It leads to the increased production of the major cold-shock proteins,… Expand
Structure of ADP·AIF4 –-stabilized nitrogenase complex and its implications for signal transduction
The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal… Expand
Molybdenum-cofactor-containing enzymes: structure and mechanism.
Molybdenum-containing enzymes catalyze basic metabolic reactions in the nitrogen, sulfur, and carbon cycles. With the exception of the nitrogenase cofactor, molybdenum is incorporated into proteins… Expand
Crystal structure of CspA, the major cold shock protein of Escherichia coli.
- H. Schindelin, W. Jiang, M. Inouye, U. Heinemann
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 24 May 1994
The major cold shock protein of Escherichia coli, CspA, produced upon a rapid downshift in growth temperature, is involved in the transcriptional regulation of at least two genes. The protein shares… Expand
The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins.
Because of mechanistic parallels in the activation of ubiquitin and the biosynthesis of several sulfur-containing cofactors, we have characterized the human Urm1 and Saccharomyces cerevisiae Uba4… Expand
Complex Formation between the Postsynaptic Scaffolding Protein Gephyrin, Profilin, and Mena: A Possible Link to the Microfilament System
- Torsten Giesemann, G. Schwarz, +8 authors B. Jockusch
- Biology, Medicine
- The Journal of Neuroscience
- 10 September 2003
Gephyrin is an essential component of the postsynaptic cortical protein network of inhibitory synapses. Gephyrin-based scaffolds participate in the assembly as well as the dynamics of receptor… Expand