1l2l
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(New page: 200px<br /><applet load="1l2l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2l, resolution 2.00Å" /> '''Crystal structure of...)
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Revision as of 18:04, 20 November 2007
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Crystal structure of ADP-dependent glucokinase from a Pyrococcus Horikoshii
Overview
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, from 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 (tlGK) 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-A translation and a 20, degrees rotation from the conserved GG sequence located at the center of, the hinge, was observed between the apo-phGK and ADP-tlGK 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.
About this Structure
1L2L is a Single protein structure of sequence from Pyrococcus horikoshii. Active as Glucokinase, with EC number 2.7.1.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-A resolution: a large conformational change in ADP-dependent glucokinase., Tsuge H, Sakuraba H, Kobe T, Kujime A, Katunuma N, Ohshima T, Protein Sci. 2002 Oct;11(10):2456-63. PMID:12237466
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