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Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum
Authors:Besir Hüseyin  Zeth Kornelius  Bracher Andreas  Heider Ursula  Ishibashi Matsujiro  Tokunaga Masao  Oesterhelt Dieter
Affiliation:Max-Planck-Institut für Biochemie, Abteilung Membranbiochemie, Am Klopferspitz 18, 82152 Martinsried, Germany. hbesir@biochem.mpg.de
Abstract:
Nucleoside diphosphate kinase from the halophilic archaeon Halobacterium salinarum was crystallized in a free state and a substrate-bound form with CDP. The structures were solved to a resolution of 2.35 and 2.2A, respectively. Crystals with the apo-form were obtained with His6-tagged enzyme, whereas the untagged form was used for co-crystallization with the nucleotide. Crosslinking under different salt and pH conditions revealed a stronger oligomerization tendency for the tagged protein at low and high salt concentrations. The influence of the His6-tag on the halophilic nature of the enzyme is discussed on the basis of the observed structural properties.
Keywords:Nucleoside diphosphate kinase   Halophilic enzyme   Halophilic adaptation   Halobacterium salinarum
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