Journal
PROTEIN SCIENCE
Volume 11, Issue 10, Pages 2456-2463Publisher
WILEY
DOI: 10.1110/ps.0215602
Keywords
crystal structure; ADP-dependent glucokinase; P. horikoshii; conformational change; induced fit
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Although ATP is the most common phosphoryl group donor for kinases, some kinases from certain hyperthermophilic archaea such as Pyrococcus horikoshii and Thermococcus litoralis use ADP as the phosphoryl donor. Those are ADP-dependent glucokinases (ADPGK) and phosphofructokinases in their glycolytic pathway. Here, we succeeded in gene cloning the ADPGK front P. horikoshii OT3 (phGK) in Escherichia coli,and in easy preparation of the enzyme, crystallization, and the structure determination of the apo enzyme. Recently, the three-dimensional structure of the ADPGK from T. litoralis (tIGK) in a complex with ADP was reported. The overall structure of two homologous enzymes (56.7%) was basically similar: This means that they consisted of large alpha/beta-domains and small domains. However, a marked adjustment of the two domains, which is a 10-Angstrom translation and a 20degrees rotation from the conserved GG sequence located at the center of the hinge, was observed between the apo-phGK and ADP-tIGK structures. The ADP-binding loop (430-439) was disordered in the apo form. It is suggested that a large conformational change takes place during the enzymatic reaction.
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