3L2I

1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium LT2.

3L2I の概要

• エントリーDOI: 10.2210/pdb3l2i/pdb
• 分子名称: 3-dehydroquinate dehydratase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: 3-dehydroquinate dehydratase, arod, shikimate pathway, idp90922, csgid, amino-acid biosynthesis, aromatic amino acid biosynthesis, lyase, schiff base, structural genomics, center for structural genomics of infectious diseases
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60226.92

構造登録者

Minasov, G.,Light, S.H.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2009-12-15, 公開日: 2009-12-29, 最終更新日: 2023-09-06)

主引用文献

Light, S.H.,Minasov, G.,Shuvalova, L.,Peterson, S.N.,Caffrey, M.,Anderson, W.F.,Lavie, A.
A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding.
Biochemistry, 50:2357-2363, 2011

PubMed Abstract: Dehydroquinate dehydratase (DHQD) catalyzes the third step in the biosynthetic shikimate pathway. We present three crystal structures of the Salmonella enterica type I DHQD that address the functionality of a surface loop that is observed to close over the active site following substrate binding. Two wild-type structures with differing loop conformations and kinetic and structural studies of a mutant provide evidence of both direct and indirect mechanisms of involvement of the loop in substrate binding. In addition to allowing amino acid side chains to establish a direct interaction with the substrate, closure of the loop necessitates a conformational change of a key active site arginine, which in turn positions the substrate productively. The absence of DHQD in humans and its essentiality in many pathogenic bacteria make the enzyme a target for the development of nontoxic antimicrobials. The structures and ligand binding insights presented here may inform the design of novel type I DHQD inhibiting molecules.

PubMed: 21291284
DOI: 10.1021/bi102020s

実験手法

X-RAY DIFFRACTION (1.85 Å)