A5080888597- Photosynthetic Processes and Mechanisms
- Mitochondrial Function and Pathology
- Enzyme Structure and Function
- Photoreceptor and optogenetics research
- ATP Synthase and ATPases Research
- Bacteriophages and microbial interactions
- Plant Virus Research Studies
- Protein Structure and Dynamics
- Electrochemical sensors and biosensors
- Hemoglobin structure and function
- RNA and protein synthesis mechanisms
- Metalloenzymes and iron-sulfur proteins
- Metal-Catalyzed Oxygenation Mechanisms
- Connexins and lens biology
- Porphyrin Metabolism and Disorders
- bioluminescence and chemiluminescence research
- Biochemical and Molecular Research
- Fungal Biology and Applications
- Peptidase Inhibition and Analysis
- Microbial Natural Products and Biosynthesis
- Viral gastroenteritis research and epidemiology
- Metabolism and Genetic Disorders
- Cancer Treatment and Pharmacology
- Synthesis and characterization of novel inorganic/organometallic compounds
- Glycosylation and Glycoproteins Research
University of Hyogo
2012-2023
Osaka University
2013-2023
Protein Research Foundation
2010-2023
Japan Science and Technology Agency
2014-2018
Centre for Research in Engineering Surface Technology
2014-2017
Hyogo University
2011-2017
Centre de Recherche en Économie et Statistique
2014
Center for Responsible Travel
2014
MRC Laboratory of Molecular Biology
1996-2011
University of Occupational and Environmental Health Japan
2009
The crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution with an R value 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl ethanolamines, three glycerols and two cholates, hemes A, copper, one magnesium, zinc. Of 3606 amino acid residues in dimer, 3560 have been converged to a reasonable by refinement. A hydrogen-bonded system, including propionate heme (heme a), part peptide backbone, imidazole ligand Cu , could provide electron...
The high resolution three-dimensional x-ray structure of the metal sites bovine heart cytochrome c oxidase is reported. Cytochrome largest membrane protein yet crystallized and analyzed at atomic resolution. Electron density distribution oxidized 2.8 Å indicates a dinuclear copper center with an unexpected similar to [2Fe-2S]-type iron-sulfur center. Previously predicted zinc magnesium have been located, former bound by nuclear encoded subunit on matrix side membrane, latter situated between...
Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, reduced, azide-bound, and carbon monoxide–bound states were determined at 2.30, 2.35, 2.9, 2.8 angstrom resolution, respectively. An aspartate residue apart from O 2 reduction site exchanges its effective accessibility to matrix aqueous phase for one cytosolic concomitantly with a significant decrease pK carboxyl group, on metal sites. The movement indicates as proton pumping site. A tyrosine acidified by...
The mitochondrial outer membrane-anchored monoamine oxidase (MAO) is a biochemically important flavoenzyme that catalyzes the deamination of biogenic and xenobiotic amines. Its two subtypes, MAOA MAOB, are linked to several psychiatric disorders therefore interesting targets for drug design. To understand relationship between structure function this enzyme, we extended our previous low-resolution rat high-resolution wild-type G110A mutant human structures at 2.2 2.17 A, respectively. similar...
Pre-MicroRNA Export Machinery Micro (mi) RNAs play a role in the regulation of many biological processes. Long transcripts are initially processed nucleus to yield pre-miRNAs that translocated through nuclear pore complex and further mature miRNAs cytoplasm. Okada et al. (p. 1275 ; see Perspective by Stewart ) describe crystal structure pre-miRNA complexed with exportin Exp5 small GTPase RanGTP. The shows RanGTP protect miRNA from degradation nucleases, as well facilitate transport RNA...
Mitochondrial cytochrome c oxidase plays an essential role in aerobic cellular respiration, reducing dioxygen to water a process coupled with the pumping of protons across mitochondrial inner membrane. An aspartate residue, Asp-51, located near enzyme surface, undergoes redox-coupled x-ray structural change, which is suggestive for this residue redox-driven proton pumping. However, functional or mechanistic evidence involvement has not yet been obtained. We report that Asp-51 → Asn mutation...
Hepatitis E virus (HEV) is a causative agent of acute hepatitis. The crystal structure HEV-like particles (HEV-LP) consisting capsid protein was determined at 3.5-A resolution. exhibited quite different folding the protruding and middle domains from members families Caliciviridae Tombusviridae, while shell domain shared common folding. Tyr-288 5-fold axis plays key roles in assembly HEV-LP, aromatic amino acid residues are well conserved among structurally related viruses. Mutational...
The OprM lipoprotein of Pseudomonas aeruginosa is a member the MexAB-OprM xenobiotic-antibiotic transporter subunits that assumed to serve as drug discharge duct across outer membrane. channel structure must differ from porin-type open pore because protein facilitates exit antibiotics but not entry. For better understanding structure-function linkage this important pump subunit, we studied x-ray crystallographic at 2.56-Å resolution. overall exhibited trimeric assembly monomer consisted...
The sterol regulatory element–binding protein 2 (SREBP-2), a nuclear transcription factor that is essential for cholesterol metabolism, enters the nucleus through direct interaction of its helix-loop-helix leucine zipper domain with importin-β. We show crystal structure importin-β complexed active form SREBP-2. Importin-β uses characteristic long helices like pair chopsticks to interact an SREBP-2 dimer. changes conformation reveal pseudo-twofold symmetry on surface so it can accommodate...
A [2Fe-2S] ferrodoxin from Spirulina platensis crystallized in space group C2221 with cell dimensions of a = 62.32, b 28.51, c 108.08 A, and alpha beta gamma 90.0 degrees. X-ray structure analysis the protein was carried out at 2.5 resolution by single isomorphous replacement method coupled derivative native anomalous dispersion methods. Phase angles 2182 independent reflections were determined their average figure merit 0.58. Each 98 residues superposed on electron density sections enlarged...
Vaults are among the largest cytoplasmic ribonucleoprotein particles and found in numerous eukaryotic species. Roles multidrug resistance innate immunity have been suggested, but cellular function remains unclear. We determined x-ray structure of rat liver vault at 3.5 angstrom resolution show that cage consists a dimer half-vaults, with each half-vault comprising 39 identical major protein (MVP) chains. Each MVP monomer folds into 12 domains: nine structural repeat domains, shoulder domain,...
The O 2 reduction site of cytochrome c oxidase (CcO), comprising iron (Fe a 3 ) and copper (Cu B ions, is probed by x-ray structural analyses CO, NO, CN - derivatives to investigate the mechanism complete . Formation derivative contributes trigonal planar coordination displaces one its three coordinated imidazole groups while water molecule becomes hydrogen bonded both ligand hydroxyl group Tyr244. When bound , it negatively polarized ( ), expected induce same change induced This allows...
When collecting data using oscillation photography, it is necessary to distinguish between those reflections which have passed completely through the Ewald sphere (`full reflections') and whose penetration incomplete (`partial reflections'). Such differentiation requires an accurate knowledge of crystal setting parameters. This particularly if partial are be used when adjacent films do not originate from same crystal. In general this case where diffracted intensities weak, as in crystals...
The fully oxidized form of cytochrome c oxidase, immediately after complete oxidation the reduced form, pumps protons upon each initial 2 single-electron reduction steps, whereas are not pumped during "as-isolated" (the without any reduction/oxidation treatment) [Bloch D, et al. (2004) catalytic cycle oxidase is sum its two halves. Proc Natl Acad Sci USA 101:529-533]. For identification structural differences causing remarkable functional difference between these distinct forms, X-ray...
Betanodaviruses cause massive mortality in marine fish species with viral nervous necrosis. The structure of a T = 3 Grouper necrosis virus-like particle (GNNV-LP) is determined by the ab initio method non-crystallographic symmetry averaging at 3.6 Å resolution. Each capsid protein (CP) shows three major domains: (i) N-terminal arm, an inter-subunit extension inner surface; (ii) shell domain (S-domain), jelly-roll structure; and (iii) protrusion (P-domain) formed three-fold trimeric...
Abstract Mitochondrial cytochrome c oxidase (C O) transfers electrons from (Cyt. ) to O 2 generate H O, a process coupled proton pumping. To elucidate the mechanism of electron transfer, we determined structure mammalian Cyt. –C complex at 2.0‐Å resolution and identified an transfer pathway C O. The specific interaction between is stabilized by few electrostatic interactions side chains within small contact surface area. Between two proteins are three water layers with long inter‐molecular...
Significance We identified hypoxia-inducible domain family, member 1A (Higd1a) as a positive regulator of cytochrome c oxidase (CcO). CcO, the terminal component mitochondrial electron transfer system, reductively converts molecular oxygen to water coupled pump protons across inner membrane. Higd1a is transiently induced under hypoxic conditions and increases CcO activity by directly interacting with in vicinity its active center. Induction leads increased consumption subsequent ATP...