1l2l
From Proteopedia
(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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| - | [[Image:1l2l.gif|left|200px]]<br /><applet load="1l2l" size=" | + | [[Image:1l2l.gif|left|200px]]<br /><applet load="1l2l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l2l, resolution 2.00Å" /> | caption="1l2l, resolution 2.00Å" /> | ||
'''Crystal structure of ADP-dependent glucokinase from a Pyrococcus Horikoshii'''<br /> | '''Crystal structure of ADP-dependent glucokinase from a Pyrococcus Horikoshii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Although ATP is the most common phosphoryl group donor for kinases, some | + | 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== | ==About this Structure== | ||
| - | 1L2L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. 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:// | + | 1L2L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. 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=1L2L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: adp glucokinase apo]] | [[Category: adp glucokinase apo]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:36 2008'' |
Revision as of 11:40, 21 February 2008
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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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