1htp

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Revision as of 17:42, 20 November 2007 by OCA (talk | contribs) (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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File:1htp.gif


1htp, resolution 2.2Å

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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 OSS 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

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