Zobrazeno 1 - 10
of 153
pro vyhledávání: '"Kazuaki Harata"'
Autor:
Hideki Katayama, Sakae Kitada, Yuichi Abe, Akio Ito, Eiichi Mizuki, Yoshitomo Kusaka, Ryuta Kanai, Tokio Ichimatsu, Kazuaki Harata, Michio Ohba, Kazuhiko Higuchi, Tetsuyuki Akao, Toshihiko Akiba
Publikováno v:
Journal of Molecular Biology. 386:121-133
Parasporin-2 is a protein toxin that is isolated from parasporal inclusions of the Gram-positive bacterium Bacillus thuringiensis. Although B. thuringiensis is generally known as a valuable source of insecticidal toxins, parasporin-2 is not insectici
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23ae9f0a030e4da37fe75ec51c7e67eb
https://doi.org/10.1016/j.jmb.2008.12.002
https://doi.org/10.1016/j.jmb.2008.12.002
Autor:
Kazuaki Harata, Ikuo Matsui
Publikováno v:
FEBS Journal. 274:4012-4022
Understanding the structural basis of thermostability and thermoactivity, and their interdependence, is central to the successful future exploitation of extremophilic enzymes in biotechnology. However, the structural basis of thermostability is still
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1aae891955eb8c67d0d7368c6fadbdf0
https://doi.org/10.1111/j.1742-4658.2007.05956.x
https://doi.org/10.1111/j.1742-4658.2007.05956.x
Autor:
Toshihiko Akiba, Kazuaki Harata, Noriyuki Ishii, Tadayuki Imanaka, Masaaki Morikawa, Naeem Rashid
Publikováno v:
Nucleic Acids Research
The X-ray crystal structure of RadB from Thermococcus kodakaraensis KOD1, an archaeal homologue of the RecA/Rad51 family proteins, have been determined in two crystal forms. The structure represents the core ATPase domain of the RecA/ Rad51 proteins.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::447b7aa05997f31d35be18f0231306eb
http://hdl.handle.net/2433/3073
http://hdl.handle.net/2433/3073
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:83-86
The reaction center-light-harvesting 1 (RC-LH1) core complex is the photosynthetic apparatus in the membrane of the purple photosynthetic bacterium Rhodopseudomonas viridis. The RC is surrounded by an LH1 complex that is constituted of oligomers of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b250461538848e5918e8a91d5698ca4
https://doi.org/10.1107/s1744309104028945
https://doi.org/10.1107/s1744309104028945
Publikováno v:
Biochemistry. 43:14047-14056
Maltohexaose-producing amylase, called G6-amylase (EC 3.2.1.98), from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) from starch and related alpha-1,4-glucans. To elucidate the reaction mechanism of G6-amylase, the enzyme activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5f5416b1d655fcb81b415777f1ede52
https://doi.org/10.1021/bi048489m
https://doi.org/10.1021/bi048489m
Autor:
Kazuaki Harata, Toshihiko Akiba
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 60:630-637
A triclinic crystal of hen egg-white lysozyme obtained from a D2O solution at 313 K was transformed into a new triclinic crystal by slow release of solvent under a temperature-regulated nitrogen-gas stream. The progress of the transition was monitore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5de8d11ee6aa1827f5d6de7e08efec55
https://doi.org/10.1107/s0907444904001805
https://doi.org/10.1107/s0907444904001805
Publikováno v:
Biochemistry. 42:14968-14976
DNA primases are essential components of the DNA replication apparatus in every organism. Reported here are the biochemical characteristics of a thermostable DNA primase from the thermophilic archaeon Pyrococcus horikoshii, which formed the oligomeri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e6e4583ca16f025701e6700cdbb719b
https://doi.org/10.1021/bi035556o
https://doi.org/10.1021/bi035556o
Autor:
Kazuaki Harata, Michiro Muraki
Publikováno v:
Journal of Molecular Recognition. 16:72-82
In spite of the belonging to the same c-type lysozyme family, hen egg-white lysozyme (HEWL) was much less susceptible to the dual-affinity labeling with 2′,3′-epoxypropyl β-glycoside of N-acetyllactosamine (Galβ1,4GlcNAc-Epo) than human lysozym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa219e6d9692ecec0fe499265c02324b
https://doi.org/10.1002/jmr.611
https://doi.org/10.1002/jmr.611
Autor:
Kazuaki Harata, Ryuta Kanai
Publikováno v:
Proteins: Structure, Function, and Genetics. 48:53-62
The crystal structure of turkey egg lysozyme (TEL) complexed with di-N-acetylchitobiose (NAG2) was refined at 1.19 A resolution by the full-matrix least-squares method with anisotropic temperature factors, and its thermal motion was evaluated by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ccbd584e8b993d2e56afc5b8ad689a0
https://doi.org/10.1002/prot.10127
https://doi.org/10.1002/prot.10127
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1569:10-20
The interactions of wheat-germ agglutinin (WGA) with the GlcNAc beta 1,6Gal sequence, a characteristic component of branched poly-N-acetyllactosaminoglycans, were investigated using isothermal titration calorimetry and X-ray crystallography. GlcNAc b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::411dc52a00d98a2cbd926d606010c300
https://doi.org/10.1016/s0304-4165(01)00231-8
https://doi.org/10.1016/s0304-4165(01)00231-8