1htp: Difference between revisions

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New page: left|200px<br /><applet load="1htp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1htp, resolution 2.2Å" /> '''REFINED STRUCTURES AT...
 
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[[Image:1htp.gif|left|200px]]<br /><applet load="1htp" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1htp.gif|left|200px]]<br /><applet load="1htp" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1htp, resolution 2.2&Aring;" />
caption="1htp, resolution 2.2&Aring;" />
'''REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX'''<br />
'''REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX'''<br />


==Overview==
==Overview==
Glycine decarboxylase consists of four protein components. Its structural, and mechanistic heart is provided by the lipoic acid-containing H-protein, which undergoes a cycle of reductive methylamination, methylamine transfer, and electron transfer. Lipoic acid attached to a specific lysine side, chain is assumed to act as a 'swinging arm' conveying the reactive, dithiolane ring from one catalytic centre to another. The X-ray crystal, structures of two forms of the H-protein have been determined. The lipoate, cofactor is located in the loop of a hairpin configuration but following, methylamine transfer it is pivoted to bind into a cleft at the surface of, the H-protein. The lipoamide-methylamine arm is, therefore, not free to, move in aqueous solvent.
Glycine decarboxylase consists of four protein components. Its structural and mechanistic heart is provided by the lipoic acid-containing H-protein which undergoes a cycle of reductive methylamination, methylamine transfer and electron transfer. Lipoic acid attached to a specific lysine side chain is assumed to act as a 'swinging arm' conveying the reactive dithiolane ring from one catalytic centre to another. The X-ray crystal structures of two forms of the H-protein have been determined. The lipoate cofactor is located in the loop of a hairpin configuration but following methylamine transfer it is pivoted to bind into a cleft at the surface of the H-protein. The lipoamide-methylamine arm is, therefore, not free to move in aqueous solvent.


==About this Structure==
==About this Structure==
1HTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with OSS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycine_dehydrogenase_(decarboxylating) Glycine dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.4.2 1.4.4.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HTP OCA].  
1HTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=OSS:'>OSS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycine_dehydrogenase_(decarboxylating) Glycine dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.4.2 1.4.4.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTP OCA].  


==Reference==
==Reference==
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[[Category: oxidoreductases(acting on ch-nh2 donor)]]
[[Category: oxidoreductases(acting on ch-nh2 donor)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:49:24 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:46 2008''