1gd9
From Proteopedia
(New page: 200px<br /><applet load="1gd9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gd9, resolution 1.8Å" /> '''CRYSTALL STRUCTURE OF...) |
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| - | [[Image:1gd9.jpg|left|200px]]<br /><applet load="1gd9" size=" | + | [[Image:1gd9.jpg|left|200px]]<br /><applet load="1gd9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gd9, resolution 1.8Å" /> | caption="1gd9, resolution 1.8Å" /> | ||
'''CRYSTALL STRUCTURE OF PYROCOCCUS PROTEIN-A1'''<br /> | '''CRYSTALL STRUCTURE OF PYROCOCCUS PROTEIN-A1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We determined the crystal structure of the liganded form of | + | We determined the crystal structure of the liganded form of alpha-aminotransferase from a hyperthermophile, Pyrococcus horikoshii. This hyperthermophilic enzyme did not show domain movement upon binding of an acidic substrate, glutamate, except for a small movement of the alpha-helix from Glu16 to Ala25. The omega-carboxyl group of the acidic substrate was recognized by Tyr70* without its side-chain movement, but not by positively charged Arg or Lys. Compared with the homologous enzymes from Thermus thermophilus HB8 and Escherichia coli, it was suggested that the more thermophilic the enzyme is, the smaller the domain movement is. This rule seems to be applicable to many other enzymes already reported. |
==About this Structure== | ==About this Structure== | ||
| - | 1GD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1GD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GD9 OCA]. |
==Reference== | ==Reference== | ||
| - | Temperature dependence of the enzyme-substrate recognition mechanism., Ura H, Harata K, Matsui I, Kuramitsu S, J Biochem | + | Temperature dependence of the enzyme-substrate recognition mechanism., Ura H, Harata K, Matsui I, Kuramitsu S, J Biochem. 2001 Jan;129(1):173-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11134972 11134972] |
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: temperature dependence of substrate recognition]] | [[Category: temperature dependence of substrate recognition]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:52 2008'' |
Revision as of 10:48, 21 February 2008
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CRYSTALL STRUCTURE OF PYROCOCCUS PROTEIN-A1
Overview
We determined the crystal structure of the liganded form of alpha-aminotransferase from a hyperthermophile, Pyrococcus horikoshii. This hyperthermophilic enzyme did not show domain movement upon binding of an acidic substrate, glutamate, except for a small movement of the alpha-helix from Glu16 to Ala25. The omega-carboxyl group of the acidic substrate was recognized by Tyr70* without its side-chain movement, but not by positively charged Arg or Lys. Compared with the homologous enzymes from Thermus thermophilus HB8 and Escherichia coli, it was suggested that the more thermophilic the enzyme is, the smaller the domain movement is. This rule seems to be applicable to many other enzymes already reported.
About this Structure
1GD9 is a Single protein structure of sequence from Pyrococcus horikoshii with as ligand. Full crystallographic information is available from OCA.
Reference
Temperature dependence of the enzyme-substrate recognition mechanism., Ura H, Harata K, Matsui I, Kuramitsu S, J Biochem. 2001 Jan;129(1):173-8. PMID:11134972
Page seeded by OCA on Thu Feb 21 12:48:52 2008
