6CPU

Crystal structure of yeast caPDE2

6CPU の概要

• エントリーDOI: 10.2210/pdb6cpu/pdb
• 分子名称: Phosphodiesterase, ZINC ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: yeast phosphodiesterase-2, hydrolase
• 由来する生物種: Candida albicans (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65683.57

構造登録者

Ke, H.,Wang, y. (登録日: 2018-03-14, 公開日: 2019-02-20, 最終更新日: 2024-04-03)

主引用文献

Yao, T.,Huang, Y.,Zhang, M.,Chen, Y.,Pei, H.,Shi, J.,Wang, H.,Wang, Y.,Ke, H.
Crystal Structures of Candida albicans Phosphodiesterase 2 and Implications for Its Biological Functions.
Biochemistry, 57:6070-6077, 2018

PubMed Abstract: The cAMP signaling system plays important roles in the physiological processes of pathogen yeast Candida albicans, but its functional mechanism has not been well illustrated. Here, we report the enzymatic characterization and crystal structures of C. albicans phosphodiesterase 2 (caPDE2) in the unliganded and 3-isobutyl-1-methylxanthine-complexed forms. caPDE2 is a monomer in liquid and crystal states and specifically hydrolyzes cAMP with a K of 35 nM. It does not effectively hydrolyze cGMP as shown by the 1.32 × 10-fold specificity of cAMP/cGMP. The crystal structure of caPDE2 shows significant differences from those of human PDEs. First, the N-terminal fragment of caPDE2 (residues 1-201) tightly associates with the catalytic domain to form a rigid molecular entity, implying its stable molecular conformation for C. albicans to resist environmental stresses. Second, the M-loop, a critical fragment for binding of the substrate and inhibitors to human PDEs, is not a part of the caPDE2 active site. This feature of caPDE2 may provide a structural basis for the design of selective inhibitors for the treatment of yeast infection.

PubMed: 30231198
DOI: 10.1021/acs.biochem.8b00707

実験手法

X-RAY DIFFRACTION (1.8 Å)