2AZ3

Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum in complex with CDP

Summary for 2AZ3

• Entry DOI: 10.2210/pdb2az3/pdb
• Related: 1NUE 2AZ1
• Descriptor: Nucleoside diphosphate kinase, MAGNESIUM ION, CYTIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: halophilic, transferase
• Biological source: Halobacterium salinarum
• Cellular location: Cytoplasm : P61136
• Total number of polymer chains: 9
• Total formula weight: 168998.81

Authors

Besir, H.,Zeth, K.,Bracher, A.,Heider, U.,Ishibashi, M.,Tokunaga, M.,Oesterhelt, D. (deposition date: 2005-09-09, release date: 2005-12-20, Last modification date: 2023-10-25)

Primary citation

Besir, H.,Zeth, K.,Bracher, A.,Heider, U.,Ishibashi, M.,Tokunaga, M.,Oesterhelt, D.
Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum
Febs Lett., 579:6595-6600, 2005

PubMed 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.

PubMed: 16293253
DOI: 10.1016/j.febslet.2005.10.052

Experimental method

X-RAY DIFFRACTION (2.2 Å)