1QO2
Crystal structure of N-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carboxamid ribonucleotid isomerase (EC 3.1.3.15, HisA)
Summary for 1QO2
Entry DOI | 10.2210/pdb1qo2/pdb |
Related | 1THF |
Descriptor | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (2 entities in total) |
Functional Keywords | isomerase, histidine biosynthesis, thermophilic protein |
Biological source | THERMOTOGA MARITIMA |
Total number of polymer chains | 2 |
Total formula weight | 54417.90 |
Authors | Wilmanns, M.,Lang, D.,Thoma, R.,Sterner, R. (deposition date: 1999-11-01, release date: 2000-07-12, Last modification date: 2024-10-23) |
Primary citation | Lang, D.,Thoma, R.,Henn-Sax, M.,Sterner, R.,Wilmanns, M. Structural Evidence for Evolution of the Beta/Alpha-Barrel Scaffold by Repeated Gene Duplication and Fusion Science, 289:1546-, 2000 Cited by PubMed Abstract: The atomic structures of two proteins in the histidine biosynthesis pathway consist of beta/alpha barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene duplication and gene fusion from a common half-barrel ancestor. These ancestral domains are not visible as independent domains in the extant proteins but can be inferred from a combination of sequence and structural analysis. The detection of subdomain structures may be useful in efforts to search genome sequences for functionally and structurally related proteins. PubMed: 10968789DOI: 10.1126/SCIENCE.289.5484.1546 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
