1I7S

ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN

1I7S の概要

• エントリーDOI: 10.2210/pdb1i7s/pdb
• 分子名称: ANTHRANILATE SYNTHASE, TRPG, TRYPTOPHAN (3 entities in total)
• 機能のキーワード: anthranilate synthase, end product inhibition, tryptophan binding, conformational change, lyase
• 由来する生物種: Serratia marcescens; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 157637.23

構造登録者

Spraggon, G.,Kim, C.,Nguyen-Huu, X.,Yee, M.-C.,Yanofsky, C.,Mills, S.E. (登録日: 2001-03-10, 公開日: 2001-05-16, 最終更新日: 2023-08-09)

主引用文献

Spraggon, G.,Kim, C.,Nguyen-Huu, X.,Yee, M.C.,Yanofsky, C.,Mills, S.E.
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
Proc.Natl.Acad.Sci.USA, 98:6021-6026, 2001

PubMed Abstract: The crystal structure of anthranilate synthase (AS) from Serratia marcescens, a mesophilic bacterium, has been solved in the presence of its substrates, chorismate and glutamine, and one product, glutamate, at 1.95 A, and with its bound feedback inhibitor, tryptophan, at 2.4 A. In comparison with the AS structure from the hyperthermophile Sulfolobus solfataricus, the S. marcescens structure shows similar subunit structures but a markedly different oligomeric organization. One crystal form of the S. marcescens enzyme displays a bound pyruvate as well as a putative anthranilate (the nitrogen group is ambiguous) in the TrpE subunit. It also confirms the presence of a covalently bound glutamyl thioester intermediate in the TrpG subunit. The tryptophan-bound form reveals that the inhibitor binds at a site distinct from that of the substrate, chorismate. Bound tryptophan appears to prevent chorismate binding by a demonstrable conformational effect, and the structure reveals how occupancy of only one of the two feedback inhibition sites can immobilize the catalytic activity of both TrpE subunits. The presence of effectors in the structure provides a view of the locations of some of the amino acid residues in the active sites. Our findings are discussed in terms of the previously described AS structure of S. solfataricus, mutational data obtained from enteric bacteria, and the enzyme's mechanism of action.

PubMed: 11371633
DOI: 10.1073/pnas.111150298

実験手法

X-RAY DIFFRACTION (2.4 Å)