1pd2: Difference between revisions

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New page: left|200px<br /><applet load="1pd2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pd2, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1pd2.gif|left|200px]]<br /><applet load="1pd2" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1pd2.gif|left|200px]]<br /><applet load="1pd2" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1pd2, resolution 2.3&Aring;" />
caption="1pd2, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE'''<br />
'''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE'''<br />


==Overview==
==Overview==
Hematopoietic prostaglandin (PG) D synthase is the key enzyme for, production of the D and J series of prostanoids in the immune system and, mast cells. We isolated a cDNA for the rat enzyme, crystallized the, recombinant enzyme, and determined the three-dimensional structure of the, enzyme complexed with glutathione at 2.3 A resolution. The enzyme is the, first member of the sigma class glutathione S-transferase (GST) from, vertebrates and possesses a prominent cleft as the active site, which is, never seen among other members of the GST family. The unique 3-D, architecture of the cleft leads to the putative substrate binding mode and, its catalytic mechanism, responsible for the specific isomerization from, PGH2 to PGD2.
Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We isolated a cDNA for the rat enzyme, crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed with glutathione at 2.3 A resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site, which is never seen among other members of the GST family. The unique 3-D architecture of the cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific isomerization from PGH2 to PGD2.


==About this Structure==
==About this Structure==
1PD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GTT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PD2 OCA].  
1PD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=GTT:'>GTT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PD2 OCA].  


==Reference==
==Reference==
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[[Category: sigma-class gst]]
[[Category: sigma-class gst]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:33 2008''