1I1Q
STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM
Summary for 1I1Q
| Entry DOI | 10.2210/pdb1i1q/pdb |
| Descriptor | ANTHRANILATE SYNTHASE COMPONENT I, ANTHRANILATE SYNTHASE COMPONENT II, TRYPTOPHAN, ... (4 entities in total) |
| Functional Keywords | tryptophan biosynthesis, lyase |
| Biological source | Salmonella typhimurium More |
| Total number of polymer chains | 2 |
| Total formula weight | 78110.01 |
| Authors | Morollo, A.A.,Eck, M.J. (deposition date: 2001-02-02, release date: 2001-04-18, Last modification date: 2024-04-03) |
| Primary citation | Morollo, A.A.,Eck, M.J. Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium. Nat.Struct.Biol., 8:243-247, 2001 Cited by PubMed Abstract: We have determined the X-ray crystal structure of the cooperative anthranilate synthase heterotetramer from Salmonella typhimurium at 1.9 A resolution with the allosteric inhibitor l-tryptophan bound to a regulatory site in the TrpE subunit. Tryptophan binding orders a loop that in turn stabilizes the inactive T state of the enzyme by restricting closure of the active site cleft. Comparison with the structure of the unliganded, noncooperative anthranilate synthase heterotetramer from Sulfolobus solfataricus shows that the two homologs have completely different quarternary structures, even though their functional dimer pairs are structurally similar, consistent with differences in the cooperative behavior of the enzymes. The structural model rationalizes mutational and biochemical studies of the enzyme and establishes the structural differences between cooperative and noncooperative anthranilate synthase homologs. PubMed: 11224570DOI: 10.1038/84988 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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