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1gc5
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(New page: 200px<br /><applet load="1gc5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gc5, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 13:48, 20 November 2007
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CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS
Overview
BACKGROUND: ATP is the most common phosphoryl group donor for kinases., However, certain hyperthermophilic archaea such as Thermococcus litoralis, and Pyrococcus furiosus utilize unusual ADP-dependent glucokinases and, phosphofructokinases in their glycolytic pathways. These ADP-dependent, kinases are homologous to each other but show no sequence similarity to, any of the hitherto known ATP-dependent enzymes. RESULTS: We solved the, crystal structure at 2.3 A resolution of an ADP-dependent glucokinase from, T. litoralis (tlGK) complexed with ADP. The overall structure can be, divided into large and small alpha/beta domains, and the ADP molecule is, buried in a shallow pocket in the large domain. Unexpectedly, the, structure was similar to those of two ATP-dependent kinases, ribokinase, and adenosine kinase. Comparison based on three-dimensional structure, revealed that several motifs important both in structure and function are, conserved, and the recognition of the alpha- and beta-phosphate of the ADP, in the tlGK was almost identical with the recognition of the beta- and, gamma-phosphate of ATP in these ATP-dependent kinases. CONCLUSIONS:, Noticeable points of our study are the first structure of ADP-dependent, kinase, the structural similarity to members of the ATP-dependent, ribokinase family, its rare nucleotide specificity caused by a shift in, nucleotide binding position by one phosphate unit, and identification of, the residues that discriminate ADP- and ATP-dependence. The strict, conservation of the binding site for the terminal and adjacent phosphate, moieties suggests a common ancestral origin of both the ATP- and, ADP-dependent kinases.
About this Structure
1GC5 is a Single protein structure of sequence from Thermococcus litoralis with ADP as ligand. Active as ADP-specific glucokinase, with EC number 2.7.1.147 Full crystallographic information is available from OCA.
Reference
Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon., Ito S, Fushinobu S, Yoshioka I, Koga S, Matsuzawa H, Wakagi T, Structure. 2001 Mar 7;9(3):205-14. PMID:11286887
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