1s3g
From Proteopedia
(New page: 200px<br /><applet load="1s3g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s3g, resolution 2.25Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1s3g.jpg|left|200px]]<br /><applet load="1s3g" size=" | + | [[Image:1s3g.jpg|left|200px]]<br /><applet load="1s3g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s3g, resolution 2.25Å" /> | caption="1s3g, resolution 2.25Å" /> | ||
'''Crystal structure of adenylate kinase from Bacillus globisporus'''<br /> | '''Crystal structure of adenylate kinase from Bacillus globisporus'''<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== | ||
| - | 1S3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_globispora Sporosarcina globispora] with ZN 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:// | + | 1S3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_globispora Sporosarcina globispora] with <scene name='pdbligand=ZN:'>ZN</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=1S3G OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Sporosarcina globispora]] | [[Category: Sporosarcina globispora]] | ||
[[Category: Bae, E.]] | [[Category: Bae, E.]] | ||
| - | [[Category: Jr., G | + | [[Category: Jr., G N.Phillips.]] |
[[Category: AP5]] | [[Category: AP5]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: psychrophile]] | [[Category: psychrophile]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:32 2008'' |
Revision as of 12:57, 21 February 2008
|
Crystal structure of adenylate kinase from Bacillus globisporus
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
1S3G is a Single protein structure of sequence from Sporosarcina globispora 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
Page seeded by OCA on Thu Feb 21 14:57:32 2008
