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 COMPLEX
Summary for 1HTP
| Entry DOI | 10.2210/pdb1htp/pdb |
| Descriptor | H-PROTEIN, 6-(HYDROXYETHYLDITHIO)-8-(AMINOMETHYLTHIO)OCTANOIC ACID (3 entities in total) |
| Functional Keywords | oxidoreductases(acting on ch-nh2 donor) |
| Biological source | Pisum sativum (pea) |
| Total number of polymer chains | 1 |
| Total formula weight | 14275.96 |
| Authors | Pares, S.,Cohen-Addad, C. (deposition date: 1995-01-11, release date: 1995-03-31, Last modification date: 2024-10-30) |
| Primary citation | Cohen-Addad, C.,Pares, S.,Sieker, L.,Neuburger, M.,Douce, R. The lipoamide arm in the glycine decarboxylase complex is not freely swinging. Nat.Struct.Biol., 2:63-68, 1995 Cited by PubMed Abstract: 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. PubMed: 7719855DOI: 10.1038/nsb0195-63 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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