6s36

Crystal structure of E. coli Adenylate kinase R119K mutant

spinqualitylabelsall models 6s36, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6s36 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MG, NA Gene: adk, D9E35_07195, D9H53_18240, D9H70_06005, D9I87_03740, EB509_06410, EB510_02065, EB515_08900, EC382_09075, ED225_07155, ED607_06260, ED611_06205, ED903_02730, ED944_09135, EEA45_02410, EF173_11005, EIA21_12240, NCTC10444_03756, NCTC9112_04001, NCTC9119_03910, NCTC9969_03944, SAMEA3472056_03545, SAMEA3485101_03900, SAMEA3485113_01288 ("Bacillus coli" Migula 1895) Activity: Adenylate kinase, with EC number 2.7.4.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A234NPI7_ECOLX] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.[HAMAP-Rule:MF_00235] Publication Abstract from PubMed As a key molecule in biology, adenosine triphosphate (ATP) has numerous crucial functions in, for instance, energetics, post-translational modifications, nucleotide biosynthesis, and cofactor metabolism. Here, we have discovered an intricate interplay between the enzyme adenylate kinase and its substrate ATP. The side chain of an arginine residue was found to be an efficient sensor of the aromatic moiety of ATP through the formation of a strong cation-pi interaction. In addition to recognition, the interaction was found to have dual functionality. First, it nucleates the activating conformational transition of the ATP binding domain and also affects the specificity in the distant AMP binding domain. In light of the functional consequences resulting from the cation-pi interaction, it is possible that the mode of ATP recognition may be a useful tool in enzyme design. Nucleation of an Activating Conformational Change by a Cation-pi Interaction.,Rogne P, Andersson D, Grundstrom C, Sauer-Eriksson E, Linusson A, Wolf-Watz M Biochemistry. 2019 Jul 29. doi: 10.1021/acs.biochem.9b00538. PMID:31339702 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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