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Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Besir, Hüseyin Zeth, Kornelius Bracher, Andreas Heider, Ursula Ishibashi, Matsujiro Tokunaga, Masao Oesterhelt, Dieter |
| Copyright Year | 2005 |
| 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. |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/j.febslet.2005.10.052 |
| PubMed reference number | 16293253 |
| Journal | Medline |
| Volume Number | 579 |
| Issue Number | 29 |
| Alternate Webpage(s) | https://files.rcsb.org/pub/pdb/validation_reports/az/2az1/2az1_full_validation.pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/j.febslet.2005.10.052 |
| Journal | FEBS letters |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
