3fb4 | pdb_00003fb4

Crystal structure of adenylate kinase from Marinibacillus marinus

spinqualitylabelsall models 3fb4, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fb4 is a 1 chain structure with sequence from Jeotgalibacillus marinus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: AP5, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6B341_9BACL Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth (By similarity).[HAMAP-Rule:MF_00235] 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 PubMed 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. Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organism Marinibacillus marinus.,Davlieva M, Shamoo Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt, 8):751-6. Epub 2009 Jul 21. PMID:19652331 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adenylate kinase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA