2az1
Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarumStructure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum
Structural highlights
FunctionNDK_HALSA Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNucleoside 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. See AlsoReferences
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