1ua4: Difference between revisions

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[[Image:1ua4.gif|left|200px]]<br /><applet load="1ua4" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ua4.gif|left|200px]]
caption="1ua4, resolution 1.90&Aring;" />
 
'''Crystal Structure of an ADP-dependent Glucokinase from Pyrococcus furiosus'''<br />
{{Structure
|PDB= 1ua4 |SIZE=350|CAPTION= <scene name='initialview01'>1ua4</scene>, resolution 1.90&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2]
|GENE=
}}
 
'''Crystal Structure of an ADP-dependent Glucokinase from Pyrococcus furiosus'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1UA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=GLC:'>GLC</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UA4 OCA].  
1UA4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UA4 OCA].  


==Reference==
==Reference==
Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase., Ito S, Fushinobu S, Jeong JJ, Yoshioka I, Koga S, Shoun H, Wakagi T, J Mol Biol. 2003 Aug 22;331(4):871-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12909015 12909015]
Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase., Ito S, Fushinobu S, Jeong JJ, Yoshioka I, Koga S, Shoun H, Wakagi T, J Mol Biol. 2003 Aug 22;331(4):871-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12909015 12909015]
[[Category: Glucokinase]]
[[Category: Glucokinase]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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[[Category: transferase]]
[[Category: transferase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:29:19 2008''

Revision as of 12:29, 20 March 2008

File:1ua4.gif


Drag the structure with the mouse to rotate
1ua4, resolution 1.90Å
Ligands: GLC and AMP
Activity: Glucokinase, with EC number 2.7.1.2
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of an ADP-dependent Glucokinase from Pyrococcus furiosus


Overview

ADP-dependent kinases are used in the modified Embden-Meyerhoff pathway of certain archaea. Our previous study has revealed a mechanism for ADP-dependent phosphoryl transfer by Thermococcus litoralis glucokinase (tlGK), and its evolutionary relationship with ATP-dependent ribokinases and adenosine kinases (PFKB carbohydrate kinase family members). Here, we report the crystal structure of glucokinase from Pyrococcus furiosus (pfGK) in a closed conformation complexed with glucose and AMP at 1.9A resolution. In comparison with the tlGK structure, the pfGK structure shows significant conformational changes in the small domain and a region around the hinge, suggesting glucose-induced domain closing. A part of the large domain next to the hinge is also shifted accompanied with domain closing. In the pfGK structure, glucose binds in a groove between the large and small domains, and the electron density of O1 atoms for both the alpha and beta-anomer configurations was observed. The structural details of the sugar-binding site of ADP-dependent glucokinase were firstly clarified and then site-directed mutagenesis analysis clarified the catalytic residues for ADP-dependent kinase, such as Arg205 and Asp451 of tlGK. Homology search and multiple alignment of amino acid sequences using the information obtained from the structures reveals that eucaryotic hypothetical proteins homologous to ADP-dependent kinases retain the residues for the recognition of a glucose substrate.

About this Structure

1UA4 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase., Ito S, Fushinobu S, Jeong JJ, Yoshioka I, Koga S, Shoun H, Wakagi T, J Mol Biol. 2003 Aug 22;331(4):871-83. PMID:12909015

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