1gc5: Difference between revisions

Revision as of 13:48, 21 February 2008

CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS

OverviewOverview

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 StructureAbout this Structure

1GC5 is a Single protein structure of sequence from Thermococcus litoralis with as ligand. Active as ADP-specific glucokinase, with EC number 2.7.1.147 Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:48:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1gc5.jpg|left|200px]]<br /><applet load="1gc5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gc5.jpg|left|200px]]<br /><applet load="1gc5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gc5, resolution 2.3&Aring;" />
 '''CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS'''<br />
 ==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.
+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==
-GC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/ADP-specific_glucokinase ADP-specific glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.147 2.7.1.147] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GC5 OCA].
+GC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/ADP-specific_glucokinase ADP-specific glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.147 2.7.1.147] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC5 OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: induced-fitting]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:55:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:34 2008''