کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2829255 1162797 2008 14 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structures of open (R) and close (T) states of prephenate dehydratase (PDT)—Implication of allosteric regulation by l-phenylalanine
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
Structures of open (R) and close (T) states of prephenate dehydratase (PDT)—Implication of allosteric regulation by l-phenylalanine
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 162, Issue 1, April 2008, Pages 94–107
نویسندگان
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