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Structure based mechanism of the Ca2+ -induced release of coelenterazine from the Renilla binding protein [Text] / G. A. Stepanyuk [et al.] // Proteins. - 2009. - Vol. 74, Is. 3. - P583-593, DOI 10.1002/prot.22173. - Cited References: 26
. - ISSN 0887-3585РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GREEN-FLUORESCENT PROTEIN
CRYSTAL-STRUCTURES
RENIFORMIS
LUCIFERASE
BIOLUMINESCENCE
PURIFICATION
ANGSTROM
MUELLERI
Кл.слова (ненормированные):
bioluminescence -- EF-hand -- coelenteramider -- luciferase -- Ca2+-binding protein
Аннотация: The crystal structure of the Ca2+-loaded coelenterazine binding protein from Renilla muelleri in its apo-state has been determined at resolution 1.8 angstrom. Although calcium binding hardly affects the compact scaffold and overall fold of the structure before calcium addition, there are easily discerned shifts in the residues that were interacting with the coelenterazine and a repositioning of helices, to expose a cavity to the external solvent. Altogether these changes offer a straightforward explanation for how following the addition of Ca2+, the coelenterazine could escape and become available for bioluminescence on Renilla luciferase. A docking computation supports the possibility of a luciferase-binding protein complex.
Держатели документа:
[Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Stepanyuk, Galina A.
Vysotski, Eugene S.
Lee, John
Rose, John P.
Wang, Bi-Cheng] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Stepanyuk, Galina A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Stepanyuk, G.A.; Liu, Z.J.; Vysotski, E.S.; Lee, J...; Rose, J.P.; Wang, B.C.
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