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Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum
Author(s) -
Besir Hüseyin,
Zeth Kornelius,
Bracher Andreas,
Heider Ursula,
Ishibashi Matsujiro,
Tokunaga Masao,
Oesterhelt Dieter
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.10.052
Subject(s) - halobacterium salinarum , halophile , nucleoside diphosphate kinase , biochemistry , haloarchaea , enzyme , chemistry , salt (chemistry) , halobacterium , nucleotide , stereochemistry , archaea , biology , bacteriorhodopsin , bacteria , organic chemistry , gene , genetics , membrane
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 2.2 Å, respectively. Crystals with the apo‐form were obtained with His 6 ‐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 His 6 ‐tag on the halophilic nature of the enzyme is discussed on the basis of the observed structural properties.