4OJV

Crystal structure of unliganded yeast PDE1

4OJV の概要

• エントリーDOI: 10.2210/pdb4ojv/pdb
• 関連するPDBエントリー: 4OJX
• 分子名称: 3',5'-cyclic-nucleotide phosphodiesterase 1, SULFATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• 機能のキーワード: phosphodiesterase, cgmp and camp, yeast pde, dual specificity, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42415.06

構造登録者

Tian, Y.,Cui, W.,Huang, M.,Robinson, H.,Wan, Y.,Wang, Y.,Ke, H. (登録日: 2014-01-21, 公開日: 2014-12-03, 最終更新日: 2024-02-28)

主引用文献

Tian, Y.,Cui, W.,Huang, M.,Robinson, H.,Wan, Y.,Wang, Y.,Ke, H.
Dual specificity and novel structural folding of yeast phosphodiesterase-1 for hydrolysis of second messengers cyclic adenosine and guanosine 3',5'-monophosphate.
Biochemistry, 53:4938-4945, 2014

PubMed Abstract: Cyclic nucleotide phosphodiesterases (PDEs) decompose second messengers cAMP and cGMP that play critical roles in many physiological processes. PDE1 of Saccharomyces cerevisiae has been subcloned and expressed in Escherichia coli. Recombinant yPDE1 has a KM of 110 μM and a kcat of 16.9 s(-1) for cAMP and a KM of 105 μM and a kcat of 11.8 s(-1) for cGMP. Thus, the specificity constant (kcat/KM(cAMP))/(kcat/KM(cGMP)) of 1.4 indicates a dual specificity of yPDE1 for hydrolysis of both cAMP and cGMP. The crystal structures of unliganded yPDE1 and its complex with GMP at 1.31 Å resolution reveal a new structural folding that is different from those of human PDEs but is partially similar to that of some other metalloenzymes such as metallo-β-lactamase. In spite of their different structures and divalent metals, yPDE1 and human PDEs may share a common mechanism for hydrolysis of cAMP and cGMP.

PubMed: 25050706
DOI: 10.1021/bi500406h

実験手法

X-RAY DIFFRACTION (1.31 Å)