A5032572885- Enzyme Structure and Function
- Protein Structure and Dynamics
- DNA Repair Mechanisms
- Metal-Catalyzed Oxygenation Mechanisms
- Biochemical and Molecular Research
- Mitochondrial Function and Pathology
- Electron Spin Resonance Studies
- Cancer Research and Treatments
- Click Chemistry and Applications
- Cellular Mechanics and Interactions
- DNA and Nucleic Acid Chemistry
- ATP Synthase and ATPases Research
- Glutathione Transferases and Polymorphisms
- Biochemical effects in animals
- RNA and protein synthesis mechanisms
- Bacterial Genetics and Biotechnology
- Nuclear Physics and Applications
- Adenosine and Purinergic Signaling
- PARP inhibition in cancer therapy
- Cholinesterase and Neurodegenerative Diseases
- Crystallization and Solubility Studies
- CRISPR and Genetic Engineering
- Photoreceptor and optogenetics research
- Advanced biosensing and bioanalysis techniques
- SARS-CoV-2 and COVID-19 Research
Nebraska Medical Center
2013-2025
University of Nebraska Medical Center
2014-2024
Stanford Synchrotron Radiation Lightsource
2001-2024
Oak Ridge National Laboratory
2017-2024
University of Nebraska at Omaha
2023
MRC Laboratory of Molecular Biology
2017
Czech Academy of Sciences
2017
University of Liverpool
2010
Ben-Gurion University of the Negev
2010
University of Kentucky
2007
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXT1.4 .ANG. Structure of Photoactive Yellow Protein, a Cytosolic Photoreceptor: Unusual Fold, Active Site, and ChromophoreGloria E. O. Borgstahl, DeWight R. Williams, Elizabeth D. GetzoffCite this: Biochemistry 1995, 34, 19, 6278–6287Publication Date (Print):May 16, 1995Publication History Published online1 May 2002Published inissue 16 1995https://pubs.acs.org/doi/10.1021/bi00019a004https://doi.org/10.1021/bi00019a004research-articleACS...
The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. atomic structure of the bleached signaling intermediate in cycle PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization 4-hydroxycinnamyl chromophore coupled rearrangements produce new set active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure protonation...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTComplete Chemical Structure of Photoactive Yellow Protein: Novel Thioester-Linked 4-Hydroxycinnamyl Chromophore and Photocycle ChemistryManuel Baca, Gloria E. O. Borgstahl, Maurice Boissinot, Patrick M. Burke, DeWight R. Williams, Kelly A. Slater, Elizabeth D. GetzoffCite this: Biochemistry 1994, 33, 48, 14369–14377Publication Date (Print):December 6, 1994Publication History Published online1 May 2002Published inissue 6 December...
Abstract Human manganese superoxide dismutase (MnSOD) is a crucial oxidoreductase that maintains the vitality of mitochondria by converting (O 2 ●− ) to molecular oxygen and hydrogen peroxide (H O with proton-coupled electron transfers (PCETs). MnSOD has evolved be highly product inhibited limit formation H , freely diffusible oxidant signaling molecule. The product-inhibited complex thought composed 2− or hydroperoxide (HO − species bound Mn ion formed from an unknown PCET mechanism....
Human manganese superoxide dismutase (MnSOD) is a homotetrameric enzyme which protects mitochondria against oxygen-mediated free radical damage. Within each subunit, both the N-terminal helical hairpin and C-terminal α/β domains contribute ligands to catalytic site. Two identical four-helix bundles, symmetrically assembled from hairpins, form novel tetrameric interface that stabilizes active sites. The 2.5 Å crystallographic structure of naturally occurring polymorphic variant Ile58Thr MnSOD...
The severe consequences of the Zika virus (ZIKV) infections resulting in congenital syndrome infants and autoimmune Guillain–Barre adults warrant development safe efficacious vaccines therapeutics. Currently, there are no approved treatment options for ZIKV infection. Herein, we describe a bacterial ferritin-based nanoparticle vaccine candidate ZIKV. viral envelope (E) protein domain III (DIII) was fused in-frame at amino-terminus ferritin. displaying DIII examined its ability to induce...
Tyrosine 34 is a prominent and conserved residue in the active site of manganese superoxide dismutases organisms from bacteria to man. We have prepared mutant containing replacement Tyr → Phe (Y34F) human dismutase (hMnSOD) crystallized it two different crystal forms, orthorhombic hexagonal. Crystal structures hMnSOD Y34F been solved 1.9 Å resolution hexagonal form, denoted as Y34Fhex, 2.2 an Y34Fortho. Both forms give that are closely superimposable with wild-type hMnSOD, phenyl rings wild...
Organophosphorus poisons (OP) bind covalently to the active-site serine of cholinesterases. The inhibited enzyme can usually be reactivated with powerful nucleophiles such as oximes. However, bound OP undergo a suicide reaction (termed aging) yielding nonreactivatable enzyme. In human butyrylcholinesterase (hBChE), aging involves residues His438 and Glu197 that are proximal (Ser198). mechanism is known in detail for nerve gases soman, sarin, tabun well pesticide metabolite isomalathion....
Abstract Human manganese superoxide dismutase is a critical oxidoreductase found in the mitochondrial matrix. Concerted proton and electron transfers are used by enzyme to rid mitochondria of O 2 •− . The mechanisms concerted transfer enzymes typically unknown due difficulties detecting protonation states specific residues solvent molecules at particular redox states. Here, neutron diffraction two redox-controlled crystals reveal all-atom structures Mn 3+ 2+ forms. deliver direct data on...
Ethylammonium nitrate (EAN) is a liquid organic salt that has many potential applications in protein chemistry. Because this solvent hydrophobic and ionic character as well the ability to hydrogen bond, it especially suited for broad use crystallography. For example, EAN may be used an additive, detergent, precipitating agent or deliver ligands into crystals. A discussion of crystallization lysozyme using given here.
The human RAD52 protein plays an important role in the earliest stages of chromosomal double-strand break repair via homologous recombination pathway. Individual subunits self-associate into rings that can then form higher order complexes. binds to DNA ends, and recent studies suggest self-association promotes end-joining. Earlier defined domain a unique region N-terminal half protein. Here we show there are fact two experimentally separable domains RAD52. mediates assembly monomers rings,...
The eukaryotic single-stranded DNA-binding protein, replication protein A (RPA), is essential in DNA metabolism and phosphorylated response to DNA-damaging agents. Rad52 RPA participate the repair of double-stranded breaks (DSBs). It known that human form a complex, but molecular mass, stoichiometry, exact role this complex DSB are unclear. In study, absolute masses individual proteins complexes were measured solution using analytical size-exclusion chromatography coupled with multiangle...
Background Post-translational modifications of histones play important roles in regulating nucleosome structure and gene transcription. It has been shown that biotinylation histone H4 at lysine-12 (K12Bio-H4) is associated with repression a number genes. We hypothesized modifies the physical nucleosomes, biotin-induced conformational changes contribute to silencing biotinylation. Methodology/Principal Findings To test this hypothesis we used atomic force microscopy directly analyze...