1p3j

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p3j.gif|left|200px]]<br /><applet load="1p3j" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1p3j.gif|left|200px]]
-
caption="1p3j, resolution 1.90&Aring;" />
+
 
-
'''Adenylate Kinase from Bacillus subtilis'''<br />
+
{{Structure
 +
|PDB= 1p3j |SIZE=350|CAPTION= <scene name='initialview01'>1p3j</scene>, resolution 1.90&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=AP5:BIS(ADENOSINE)-5'-PENTAPHOSPHATE'>AP5</scene>
 +
|ACTIVITY= [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]
 +
|GENE= ADK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
 +
}}
 +
 
 +
'''Adenylate Kinase from Bacillus subtilis'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
1P3J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3J OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15100224 15100224]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/15100224 15100224]
[[Category: Adenylate kinase]]
[[Category: Adenylate kinase]]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
Line 21: Line 30:
[[Category: zinc coordination]]
[[Category: zinc coordination]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:43 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:19:23 2008''

Revision as of 11:19, 20 March 2008


PDB ID 1p3j

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , and
Gene: ADK (Bacillus subtilis)
Activity: Adenylate kinase, with EC number 2.7.4.3
Coordinates: save as pdb, mmCIF, xml



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. 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 Mar 20 13:19:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools