2QMX

The crystal structure of L-Phe inhibited prephenate dehydratase from Chlorobium tepidum TLS

2QMX の概要

• エントリーDOI: 10.2210/pdb2qmx/pdb
• 分子名称: Prephenate dehydratase, ACETATE ION, PHENYLALANINE, ... (5 entities in total)
• 機能のキーワード: apc86053, l-phe inhibition, prephenate dehydratase, pdt, chlorobium tepidum tls, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, lyase, ligase
• 由来する生物種: Chlorobium tepidum TLS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64323.52

構造登録者

Tan, K.,Li, H.,Clancy, S.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2007-07-17, 公開日: 2007-08-07, 最終更新日: 2024-11-13)

主引用文献

Tan, K.,Li, H.,Zhang, R.,Gu, M.,Clancy, S.T.,Joachimiak, A.
Structures of open (R) and close (T) states of prephenate dehydratase (PDT) - implication of allosteric regulation by L-phenylalanine.
J.Struct.Biol., 162:94-107, 2008

PubMed Abstract: The enzyme prephenate dehydratase (PDT) converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis. PDT is allosterically regulated by L-Phe and other amino acids. We report the first crystal structures of PDT from Staphylococcus aureus in a relaxed (R) state and PDT from Chlorobium tepidum in a tense (T) state. The two enzymes show low sequence identity (27.3%) but the same prototypic architecture and domain organization. Both enzymes are tetramers (dimer of dimers) in crystal and solution while a PDT dimer can be regarded as a basic catalytic unit. The N-terminal PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In one PDT dimer two clefts are aligned to form an extended active site across the dimer interface. Similarly at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation.

PubMed: 18171624
DOI: 10.1016/j.jsb.2007.11.009

実験手法

X-RAY DIFFRACTION (2.3 Å)