Publication Abstract from PubMed
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.
Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum.,Besir H, Zeth K, Bracher A, Heider U, Ishibashi M, Tokunaga M, Oesterhelt D FEBS Lett. 2005 Dec 5;579(29):6595-600. Epub 2005 Nov 9. PMID:16293253[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
