1p3j
From Proteopedia
(New page: 200px<br /><applet load="1p3j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p3j, resolution 1.90Å" /> '''Adenylate Kinase fro...) |
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| - | [[Image:1p3j.gif|left|200px]]<br /><applet load="1p3j" size=" | + | [[Image:1p3j.gif|left|200px]]<br /><applet load="1p3j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p3j, resolution 1.90Å" /> | caption="1p3j, resolution 1.90Å" /> | ||
'''Adenylate Kinase from Bacillus subtilis'''<br /> | '''Adenylate Kinase from Bacillus subtilis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of adenylate kinases from the psychrophile Bacillus | + | The crystal structures of adenylate kinases from the psychrophile Bacillus globisporus and the mesophile Bacillus subtilis have been solved and compared with that from the thermophile Bacillus stearothermophilus. This is the first example we know of where a trio of protein structures has been solved that have the same number of amino acids and a high level of identity (66-74%) and yet come from organisms with different operating temperatures. The enzymes were characterized for their own thermal denaturation and inactivation, and they exhibited the same temperature preferences as their source organisms. The structures of the three highly homologous, dynamic proteins with different temperature-activity profiles provide an opportunity to explore a molecular mechanism of cold and heat adaptation. Their analysis suggests that the maintenance of the balance between stability and flexibility is crucial for proteins to function at their environmental temperatures, and it is achieved by the modification of intramolecular interactions in the process of temperature adaptation. |
==About this Structure== | ==About this Structure== | ||
| - | 1P3J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN, MG and AP5 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] Full crystallographic information is available from [http:// | + | 1P3J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=AP5:'>AP5</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bae, E.]] | [[Category: Bae, E.]] | ||
| - | [[Category: Jr., G | + | [[Category: Jr., G N.Phillips.]] |
[[Category: AP5]] | [[Category: AP5]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: zinc coordination]] | [[Category: zinc coordination]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:43 2008'' |
Revision as of 12:24, 21 February 2008
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Adenylate Kinase from Bacillus subtilis
Overview
The crystal structures of adenylate kinases from the psychrophile Bacillus globisporus and the mesophile Bacillus subtilis have been solved and compared with that from the thermophile Bacillus stearothermophilus. This is the first example we know of where a trio of protein structures has been solved that have the same number of amino acids and a high level of identity (66-74%) and yet come from organisms with different operating temperatures. The enzymes were characterized for their own thermal denaturation and inactivation, and they exhibited the same temperature preferences as their source organisms. The structures of the three highly homologous, dynamic proteins with different temperature-activity profiles provide an opportunity to explore a molecular mechanism of cold and heat adaptation. Their analysis suggests that the maintenance of the balance between stability and flexibility is crucial for proteins to function at their environmental temperatures, and it is achieved by the modification of intramolecular interactions in the process of temperature adaptation.
About this Structure
1P3J is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Active as Adenylate kinase, with EC number 2.7.4.3 Full crystallographic information is available from OCA.
Reference
Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases., Bae E, Phillips GN Jr, J Biol Chem. 2004 Jul 2;279(27):28202-8. Epub 2004 Apr 20. PMID:15100224
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