1htp
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| , resolution 2.2Å | |||||||
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| Ligands: | |||||||
| Activity: | Glycine dehydrogenase (decarboxylating), with EC number 1.4.4.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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