1htp: Difference between revisions

Revision as of 08:39, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1htp.png

Template:STRUCTURE 1htp

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 COMPLEXREFINED 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

Template:ABSTRACT PUBMED 7719855

About this StructureAbout this Structure

1HTP is a Single protein structure of sequence from Pisum sativum. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1htp.gif|left|200px]]
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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'''
+===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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