1I1Q

STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM

1I1Q の概要

• エントリーDOI: 10.2210/pdb1i1q/pdb
• 分子名称: ANTHRANILATE SYNTHASE COMPONENT I, ANTHRANILATE SYNTHASE COMPONENT II, TRYPTOPHAN, ... (4 entities in total)
• 機能のキーワード: tryptophan biosynthesis, lyase
• 由来する生物種: Salmonella typhimurium; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78110.01

構造登録者

Morollo, A.A.,Eck, M.J. (登録日: 2001-02-02, 公開日: 2001-04-18, 最終更新日: 2024-04-03)

主引用文献

Morollo, A.A.,Eck, M.J.
Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.
Nat.Struct.Biol., 8:243-247, 2001

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: 11224570
DOI: 10.1038/84988

実験手法

X-RAY DIFFRACTION (1.9 Å)