Crystal structure of shrimp arginine kinase in binary complex with arginine - A molecular view of the phosphagen precursor binding to the enzyme

Alonso A. López-Zavala, Karina D. García-Orozco, Jesús S. Carrasco-Miranda, Rocio Sugich-Miranda, Enrique F. Velázquez-Contreras, Michael F. Criscitiello, Luis G. Brieba, Enrique Rudiño-Piñera, Rogerio R. Sotelo-Mundo

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Arginine kinase (AK) is a key enzyme for energetic balance in invertebrates. Although AK is a well-studied system that provides fast energy to invertebrates using the phosphagen phospho-arginine, the structural details on the AK-arginine binary complex interaction remain unclear. Herein, we determined two crystal structures of the Pacific whiteleg shrimp (Litopenaeus vannamei) arginine kinase, one in binary complex with arginine (LvAK-Arg) and a ternary transition state analog complex (TSAC). We found that the arginine guanidinium group makes ionic contacts with Glu225, Cys271 and a network of ordered water molecules. On the zwitterionic side of the amino acid, the backbone amide nitrogens of Gly64 and Val65 coordinate the arginine carboxylate. Glu314, one of proposed acid-base catalytic residues, did not interact with arginine in the binary complex. This residue is located in the flexible loop 310-320 that covers the active site and only stabilizes in the LvAK-TSAC. This is the first binary complex crystal structure of a guanidine kinase in complex with the guanidine substrate and could give insights into the nature of the early steps of phosphagen biosynthesis. © 2013 Springer Science+Business Media New York.
Original languageAmerican English
Pages (from-to)511-518
Number of pages8
JournalJournal of Bioenergetics and Biomembranes
DOIs
StatePublished - 1 Dec 2013

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