2zf5: Difference between revisions

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[[Image:2zf5.jpg|left|200px]]
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{{STRUCTURE_2zf5|  PDB=2zf5  |  SCENE=  }}  
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'''Crystal Structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon'''
===Crystal Structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon===




==Overview==
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The crystal structure of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis (Tk-GK) in a dimeric form was determined at a resolution of 2.4 A. This is the first crystal structure of a hyperthermophilic glycerol kinase. The overall structure of the Tk-GK dimer is very similar to that of the Escherichia coli glycerol kinase (Ec-GK) dimer. However, two dimers of Ec-GK can associate into a tetramer with a twofold axis, whereas those of Tk-GK cannot. This may be the reason why Tk-GK is not inhibited by fructose 1,6-bisphosphate, because the fructose 1,6-bisphosphate binding site is produced only when a tetrameric structure is formed. Differential scanning calorimetry analyses indicate that Tk-GK is a highly thermostable protein with a melting temperature (T(m)) of 105.4 degrees C for the major transition. This value is higher than that of Ec-GK by 34.1 degrees C. Comparison of the crystal structures of Tk-GK and Ec-GK indicate that there is a marked difference in the number of ion pairs in the alpha16 helix. Four ion pairs, termed IP1-IP4, are formed in this helix in the Tk-GK structure. To examine whether these ion pairs contribute to the stabilization of Tk-GK, four Tk-GK and four Ec-GK derivatives with reciprocal mutations at the IP1-IP4 sites were constructed. The determination of their stabilities indicates that the removal of each ion pair does not affect the stability of Tk-GK significantly, whereas the mutations designed to introduce one of these ion pairs stabilize or destabilize Ec-GK considerably. These results suggest that the ion pairs in the alpha16 helix contribute to the stabilization of Tk-GK in a cooperative manner.
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==About this Structure==
==About this Structure==
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[[Category: Nucleotide-binding]]
[[Category: Nucleotide-binding]]
[[Category: Transferase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  7 08:51:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:55:09 2008''

Revision as of 08:55, 29 July 2008

File:2zf5.png

Template:STRUCTURE 2zf5

Crystal Structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon

Template:ABSTRACT PUBMED 18422647

About this Structure

2ZF5 is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.

Reference

Crystal structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon in a dimeric form., Koga Y, Katsumi R, You DJ, Matsumura H, Takano K, Kanaya S, FEBS J. 2008 May;275(10):2632-43. Epub 2008 Apr 17. PMID:18422647

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