1htp: Difference between revisions

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-[[Image:1htp.gif|left|200px]]
+{{Seed}}
+[[Image:1htp.png|left|200px]]
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 {{STRUCTURE_1htp|  PDB=1htp  |  SCENE=  }}
-'''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'''
+===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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7719855}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7719855 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7719855}}
 ==About this Structure==
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 [[Category: Cohen-Addad, C.]]
 [[Category: Pares, S.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:13:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:39:50 2008''