Intermediate Phosphorylation Reactions in the Mechanism of ATP Utilization by the Copper ATPase (CopA) of Thermotoga maritima

Autor: Giuseppe Inesi, Yuta Hatori, Chikashi Toyoshima, Rajendra Pilankatta, Ayami Hirata, David Lewis

Publikováno v: The Journal of Biological Chemistry

Recombinant and purified Thermotoga maritima CopA sustains ATPase velocity of 1.78-2.73 micromol/mg/min in the presence of Cu+ (pH 6, 60 degrees C) and 0.03-0.08 micromol/mg/min in the absence of Cu+. High levels of enzyme phosphorylation are obtaine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd104a27dd3525435994fd4957899a5e
https://doi.org/10.1074/jbc.m802735200

Sequential substitution of K+ bound to Na+,K+-ATPase visualized by X-ray crystallography

Autor: Haruo Ogawa, Chikashi Toyoshima, Ayami Hirata, Flemming Cornelius

Publikováno v: Ogawa, H, Cornelius, F, Hirata, A & Toyoshima, C 2015, ' Sequential substitution of K+ bound to Na+,K+-ATPase visualized by X-ray crystallography ', Nature Communications .
Nature Communications

Na+,K+-ATPase transfers three Na+ from the cytoplasm into the extracellular medium and two K+ in the opposite direction per ATP hydrolysed. The binding and release of Na+ and K+ are all thought to occur sequentially. Here we demonstrate by X-ray crys

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cbe5935e9aa255425223e5801f31d4f
https://pure.au.dk/portal/da/publications/sequential-substitution-of-k-bound-to-nakatpase-visualized-by-xray-crystallography(43738407-1196-415e-905c-b0506691d20a).html

ChemInform Abstract: Crystal Structures of the Calcium Pump and Sarcolipin in the Mg2+-Bound E1 State

Autor: Giuseppe Inesi, Chikashi Toyoshima, Junko Tsueda, Haruo Ogawa, Ayami Hirata, Shiho Iwasawa

Publikováno v: ChemInform. 44

The X-ray crystal structures of SERCA1a, a Ca2+-ATPase from the sarcoplasmic reticulum, in the presence and absence of sarcolipin are reported; the structures indicate that sarcolipin stabilizes SERCA1a in an ‘open’ state that has not been well c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a1a9ef91cfa43ee004fa8f42362dbeb8
https://doi.org/10.1002/chin.201321269

Conformational fluctuations of the Ca2+-ATPase in the native membrane environment. Effects of pH, temperature, catalytic substrates, and thapsigargin

Autor: Giuseppe, Inesi, David, Lewis, Chikashi, Toyoshima, Ayami, Hirata, Leopoldo, de Meis

Publikováno v: The Journal of biological chemistry. 283(2)

Digestion with proteinase K or trypsin yields complementary information on conformational transitions of the Ca(2+)-ATPase (SERCA) in the native membrane environment. Distinct digestion patterns are obtained with proteinase K, revealing interconversi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c41615bd9c3d8caafbdc1e8cb532f362
https://pubmed.ncbi.nlm.nih.gov/17993458

Visualization of lipid bilayer in the crystals by solvent contrast modulation

Autor: Ayami Hirata, Chikashi Toyoshima, Yoshiyuki Norimatsu, Junko Tsueda, Shiho Iwasawa

Publikováno v: Acta Crystallographica Section A Foundations and Advances. 70:C1498-C1498

A new method of X-ray solvent contrast modulation was developed to visualize lipid bilayers in crystals of membrane proteins at a high enough resolution to resolve individual phospholipids molecules (~3.5 Å ). Visualization of lipid bilayer has been

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9a4e52a14cd7a51ec71ef6709004dea3
https://doi.org/10.1107/s2053273314085015