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5XZ2

Crystal structure of adenylate kinase

Summary for 5XZ2
Entry DOI10.2210/pdb5xz2/pdb
DescriptorAdenylate kinase isoenzyme 1, BIS(ADENOSINE)-5'-PENTAPHOSPHATE, SULFATE ION, ... (4 entities in total)
Functional Keywordsphosphorylation, transferase
Biological sourceDanio rerio (Zebrafish)
Total number of polymer chains2
Total formula weight45365.02
Authors
Moon, S.,Bae, E.,Kim, J. (deposition date: 2017-07-11, release date: 2018-07-18, Last modification date: 2023-11-22)
Primary citationMoon, S.,Kim, J.,Bae, E.
Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes
Sci Rep, 7:16027-16027, 2017
Cited by
PubMed Abstract: Psychrophiles are extremophilic organisms capable of thriving in cold environments. Proteins from these cold-adapted organisms can remain physiologically functional at low temperatures, but are structurally unstable even at moderate temperatures. Here, we report the crystal structure of adenylate kinase (AK) from the Antarctic fish Notothenia coriiceps, and identify the structural basis of cold adaptation by comparison with homologues from tropical fishes including Danio rerio. The structure of N. coriiceps AK (AKNc) revealed suboptimal hydrophobic packing around three Val residues in its central CORE domain, which are replaced with Ile residues in D. rerio AK (AKDr). The Val-to-Ile mutations that improve hydrophobic CORE packing in AKNc increased stability at high temperatures but decreased activity at low temperatures, suggesting that the suboptimal hydrophobic CORE packing is important for cold adaptation. Such linkage between stability and activity was also observed in AKDr. Ile-to-Val mutations that destabilized the tropical AK resulted in increased activity at low temperatures. Our results provide the structural basis of cold adaptation of a psychrophilic enzyme from a multicellular, eukaryotic organism, and highlight the similarities and differences in the structural adjustment of vertebrate and bacterial psychrophilic AKs during cold adaptation.
PubMed: 29167503
DOI: 10.1038/s41598-017-16266-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

229380

數據於2024-12-25公開中

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