3FB4

Crystal structure of adenylate kinase from Marinibacillus marinus

Summary for 3FB4

• Entry DOI: 10.2210/pdb3fb4/pdb
• Related: 1S3G
• Descriptor: Adenylate kinase, ZINC ION, BIS(ADENOSINE)-5'-PENTAPHOSPHATE, ... (4 entities in total)
• Functional Keywords: psychrophile, kinase, adenylate kinase, phosphotransferase, atp-binding, nucleotide-binding, transferase
• Biological source: Marinibacillus marinus
• Cellular location: Cytoplasm (By similarity): Q6B341
• Total number of polymer chains: 1
• Total formula weight: 25053.45

Authors

Davlieva, M.G.,Shamoo, Y. (deposition date: 2008-11-18, release date: 2009-09-29, Last modification date: 2023-09-06)

Primary citation

Davlieva, M.,Shamoo, Y.
Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organism Marinibacillus marinus.
Acta Crystallogr.,Sect.F, 65:751-756, 2009

PubMed Abstract: Adenylate kinases (AKs; EC 2.7.4.3) are essential members of the NMP kinase family that maintain cellular homeostasis by the interconversion of AMP, ADP and ATP. AKs play a critical role in adenylate homeostasis across all domains of life and have been used extensively as prototypes for the study of protein adaptation and the relationship of protein dynamics and stability to function. To date, kinetic studies of psychrophilic AKs have not been performed. In order to broaden understanding of extremophilic adaptation, the kinetic parameters of adenylate kinase from the psychrophile Marinibacillus marinus were examined and the crystal structure of this cold-adapted enzyme was determined at 2.0 A resolution. As expected, the overall structure and topology of the psychrophilic M. marinus AK are similar to those of mesophilic and thermophilic AKs. The thermal denaturation midpoint of M. marinus AK (321.1 K) is much closer to that of the mesophile Bacillus subtilis (320.7 K) than the more closely related psychrophile B. globisporus (316.4 K). In addition, the enzymatic properties of M. marinus AK are quite close to those of the mesophilic AK and suggests that M. marinus experiences temperature ranges in which excellent enzyme function over a broad temperature range (293-313 K) has been retained for the success of the organism. Even transient loss of AK function is lethal and as a consequence AK must be robust and be well adapted to the environment of the host organism.

PubMed: 19652331
DOI: 10.1107/S1744309109024348

Experimental method

X-RAY DIFFRACTION (2 Å)