4BG4

Crystal structure of Litopenaeus vannamei arginine kinase in a ternary analog complex with arginine, ADP-Mg and NO3

Summary for 4BG4

• Entry DOI: 10.2210/pdb4bg4/pdb
• Descriptor: ARGININE KINASE, ADENOSINE-5'-DIPHOSPHATE, ARGININE, ... (8 entities in total)
• Functional Keywords: transferase, binary complex
• Biological source: LITOPENAEUS VANNAMEI (PACIFIC WHITE SHRIMP); More
• Total number of polymer chains: 2
• Total formula weight: 82009.32

Authors

Lopez-Zavala, A.A.,Garcia-Orozco, K.D.,Carrasco-Miranda, J.S.,Sugich-Miranda, R.,Velazquez-Contreras, E.F.,Criscitiello, M.F.,GBrieba, L.,Rudino-Pinera, E.,Sotelo-Mundo, R.R. (deposition date: 2013-03-22, release date: 2013-09-04, Last modification date: 2023-12-20)

Primary citation

Lopez-Zavala, A.A.,Garcia-Orozco, K.D.,Carrasco-Miranda, J.S.,Sugich-Miranda, R.,Velazquez-Contreras, E.F.,Criscitiello, M.F.,Brieba, L.G.,Rudino-Pinera, E.,Sotelo-Mundo, R.R.
Crystal Structure of Shrimp Arginine Kinase in Binary Complex with Arginine-A Molecular View of the Phosphagen Precursor Binding to the Enzyme.
J.Bioenerg.Biomembr., 45:511-, 2013

PubMed 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.

PubMed: 23873077
DOI: 10.1007/S10863-013-9521-0

Experimental method

X-RAY DIFFRACTION (1.601 Å)