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| | {{STRUCTURE_1gc5| PDB=1gc5 | SCENE= }} | | {{STRUCTURE_1gc5| PDB=1gc5 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS'''
| + | ===CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11286887}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11286887 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11286887}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Alfa/beta sandwich]] | | [[Category: Alfa/beta sandwich]] |
| | [[Category: Induced-fitting]] | | [[Category: Induced-fitting]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:24:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:03:57 2008'' |
Revision as of 02:03, 1 July 2008
Template:STRUCTURE 1gc5
CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS
Template:ABSTRACT PUBMED 11286887
About this Structure
1GC5 is a Single protein structure of sequence from Thermococcus litoralis. 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
Page seeded by OCA on Tue Jul 1 05:03:57 2008
