2QMW

The crystal structure of the prephenate dehydratase (PDT) from Staphylococcus aureus subsp. aureus Mu50

Replaces:  2IQ8

Summary for 2QMW

• Entry DOI: 10.2210/pdb2qmw/pdb
• Descriptor: Prephenate dehydratase, SODIUM ION, ACETATE ION, ... (6 entities in total)
• Functional Keywords: apc85812, prephenate dehydratase (pdt), staphylococcus aureus subsp. aureus mu50, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• Biological source: Staphylococcus aureus subsp. aureus
• Total number of polymer chains: 2
• Total formula weight: 60318.28

Authors

Tan, K.,Zhang, R.,Li, H.,Gu, M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2007-07-17, release date: 2007-08-07, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)