A5020639714- Enzyme Structure and Function
- Endoplasmic Reticulum Stress and Disease
- Ubiquitin and proteasome pathways
- Biochemical and Molecular Research
- Metalloenzymes and iron-sulfur proteins
- Neuroscience and Neuropharmacology Research
- Glycosylation and Glycoproteins Research
- Peptidase Inhibition and Analysis
- RNA modifications and cancer
- Cellular transport and secretion
- Protein Structure and Dynamics
- Metal-Catalyzed Oxygenation Mechanisms
- Amino Acid Enzymes and Metabolism
- Electrocatalysts for Energy Conversion
- RNA and protein synthesis mechanisms
- Protein Kinase Regulation and GTPase Signaling
- Alkaline Phosphatase Research Studies
- Autophagy in Disease and Therapy
- Photosynthetic Processes and Mechanisms
- Chemical Synthesis and Analysis
- Folate and B Vitamins Research
- Nicotinic Acetylcholine Receptors Study
- Porphyrin Metabolism and Disorders
- Cancer, Hypoxia, and Metabolism
- Porphyrin and Phthalocyanine Chemistry
University of Würzburg
2016-2025
University of Chicago
2012
Northwestern University
2009
University of Georgia
2009
Stony Brook University
1998-2008
University of Potsdam
2008
State University of New York
1999-2007
University Medical Center
2006-2007
Duke University
2006-2007
California Institute of Technology
1996-2006
The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been implicated in cloud nucleation and global climate regulation. crystal structure DMSO from Rhodobacter sphaeroides reveals monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides asymmetrically coordinate through their dithiolene groups. One pterins exhibits different coordination modes between oxidized reduced states, whereas side chain oxygen...
The major cold shock protein of Escherichia coli, CspA, produced upon a rapid downshift in growth temperature, is involved the transcriptional regulation at least two genes. shares high homology with nucleic acid-binding domain Y-box factors, family eukaryotic proteins and translational regulation. crystal structure CspA has been determined 2-A resolution refined to R = 0.187. composed five antiparallel beta-strands forming closed five-stranded beta-barrel. three-dimensional similar that...
The MoaA and MoaC proteins catalyze the first step during molybdenum cofactor biosynthesis, conversion of a guanosine derivative to precursor Z. belongs S -adenosylmethionine (SAM)-dependent radical enzyme superfamily, members which formation protein and/or substrate radicals by reductive cleavage SAM [4Fe–4S] cluster. A defined in vitro system is described, generates Z led identification 5′-GTP as substrate. structures apo-state (2.8 Å) complex with (2.2 provide valuable insights into its...
The majority of fast synaptic inhibition in the brain is mediated by benzodiazepine-sensitive α1-subunit-containing GABA type A receptors (GABA Rs); however, our knowledge mechanisms neurons use to regulate their accumulation rudimentary. Using immunoprecipitation, we demonstrate that Rs and gephyrin are intimately associated at inhibitory synapses cultured rat neurons. In vitro reveal E-domain directly binds α1 subunit with an affinity ∼20 μ m , residues 360–375 within intracellular domain...
GABAA receptors are clustered at synaptic sites to achieve a high density of postsynaptic opposite the input axonal terminals. This allows an efficient propagation GABA mediated signals, which mostly result in neuronal inhibition. A key organizer for inhibitory is 93 kDa protein gephyrin that forms oligomeric superstructures beneath area. Gephyrin has long been known be directly associated with glycine receptor β subunits mediate inhibition spinal cord. Recently, have also shown interact...
The first step in molybdenum cofactor biosynthesis, the conversion of 5'-GTP to precursor Z, an oxygen-sensitive tetrahydropyranopterin is catalyzed by S-adenosylmethionine (SAM)-dependent enzyme MoaA and accessory protein MoaC. This reaction involves radical-initiated intramolecular rearrangement guanine C8 atom. harbors N-terminal [4Fe-4S] cluster, which involved reductive cleavage SAM generates a 5'-deoxyadenosyl radical (5'-dA*), C-terminal cluster presumably substrate binding and/or...
The human proteins MOCS1A and MOCS1B catalyze the conversion of a guanosine derivative to precursor Z during molybdenum cofactor biosynthesis. shares homology with S-adenosylmethionine (AdoMet)-dependent radical enzymes, which formation protein and/or substrate radicals by reductive cleavage AdoMet through [4Fe-4S] cluster. Sequence analysis showed two highly conserved cysteine motifs, one near N terminus C terminus. was heterologously expressed in Escherichia coli purified under aerobic...
Acid-sensing ion channels are ligand-gated cation channels, gated by extracellular H(+). H(+) is the simplest ligand possible, and whereas for larger ligands that gate complex binding sites in three-dimensional structure of proteins have to be assumed, could principle a channel titration single amino acid. Experimental evidence suggests more situation, however. For example, it has been shown Ca(2+) ions compete with H(+); probably bound loop ASICs stabilize closed state displaced before can...
Several lines of evidence suggest that G-protein-coupled receptors can adopt different active conformations, but their direct demonstration in intact cells is still missing. Using a fluorescence resonance energy transfer (FRET)-based approach we studied conformational changes α<sub>2A</sub>-adrenergic cells. The were C-terminally labeled with cyan fluorescent protein and fluorescein arsenical hairpin binder at sites the third intracellular loop: N-terminally close to transmembrane domain V...
Gephyrin is the major protein determinant for clustering of inhibitory neurotransmitter receptors. Earlier analyses revealed that gephyrin tightly binds to residues 398-410 glycine receptor β subunit (GlyR β) and, as demonstrated only recently, also interacts with GABA(A) receptors (GABA(A)Rs) containing α1, α2, and α3 subunits. Here, we dissect molecular basis underlying interactions between GABA(A)Rs these α-subunits compare them crystal structure gephyrin-GlyR complex. Biophysical...
The multifunctional scaffolding protein gephyrin is a key player in the formation of postsynaptic scaffold at inhibitory synapses, clustering both glycine receptors (GlyRs) and selected GABA(A) receptor (GABA(A)R) subtypes. We report direct interaction between GABA(A)R α3 subunit gephyrin, mapping reciprocal binding sites using mutagenesis, overlay, yeast two-hybrid assays. This analysis reveals that critical determinants this are located motif FNIVGTTYPI M3-M4 domain SMDKAFITVL N terminus E...