6s36

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Crystal structure of E. coli Adenylate kinase R119K mutant

Structural highlights

6s36 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:CL, MG, NA
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KAD_ECOLI 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.[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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Rogne P, Andersson D, Grundstrom C, Sauer-Eriksson E, Linusson A, Wolf-Watz M. Nucleation of an Activating Conformational Change by a Cation-pi Interaction. Biochemistry. 2019 Jul 29. doi: 10.1021/acs.biochem.9b00538. PMID:31339702 doi:http://dx.doi.org/10.1021/acs.biochem.9b00538

Contents


PDB ID 6s36

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