1htp: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
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...
 
No edit summary
Line 1: Line 1:
[[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==
Line 19: Line 19:
[[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''

Revision as of 14:04, 21 February 2008

File:1htp.gif


1htp, resolution 2.2Å

Drag the structure with the mouse to rotate

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

OverviewOverview

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 StructureAbout this Structure

1HTP is a Single protein structure of sequence from Pisum sativum with as ligand. Active as Glycine dehydrogenase (decarboxylating), with EC number 1.4.4.2 Full crystallographic information is available from OCA.

ReferenceReference

The lipoamide arm in the glycine decarboxylase complex is not freely swinging., Cohen-Addad C, Pares S, Sieker L, Neuburger M, Douce R, Nat Struct Biol. 1995 Jan;2(1):63-8. PMID:7719855

Page seeded by OCA on Thu Feb 21 13:04:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA