Structural and functional identification of the uncharacterized metallo-beta-lactamase superfamily protein TW9814 as a phosphodiesterase with unique metal coordination

Heo Yunseok; Park Soo Bong; Jeon Ye EunYun Ji HyeJeong Bo GyeongCha Sun ShinLee Weontae

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Structural and functional identification of the uncharacterized metallo-beta-lactamase superfamily protein TW9814 as a phosphodiesterase with unique metal coordination

机译：结构和功能的识别但一个个金属-β-内酰胺酶总科蛋白质TW9814磷酸二酯酶具有独特的金属协调

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Metallo-beta-lactamase (MBL) superfamily proteins have a common alpha beta/beta alpha sandwich fold and perform a variety of functions through metal-mediated catalysis. However, because of the enormous scale of this superfamily, only a small percentage of the proteins belonging to the superfamily have been annotated structurally or functionally to date. Therefore, much remains unknown about the MBL superfamily proteins. Here, TW9814, a hypothetical MBL superfamily protein, was structurally and functionally investigated. Guided by the crystal structure of dimeric TW9814, it was demonstrated that TW9814 functions as a phosphodiesterase (PDE) in the presence of divalent metal ions such as manganese(II) or nickel(II). A docking model between TW9814 and the substrate bis(p-nitrophenyl)phosphate (bpNPP) showed the importance of the dimerization of TW9814 for its bpNPP-hydrolyzing activity and for the interaction between the enzyme and the substrate. TW9814 showed outstanding catalytic efficiency (k(cat)/K-m) under alkaline conditions compared with other PDEs. The activity of TW9814 appears to be regulated through a disulfide bond, which is a feature that is not present in other MBL superfamily members. This study provides a platform for the functional characterization of other hypothetical proteins of the MBL or other superfamilies.

机译：金属-β-内酰胺酶(MBL)总科的蛋白质有一个共同的αβα/β三明治折叠和执行各种功能metal-mediated催化。大规模的总科,只有一个小比例的蛋白质属于带注释的结构或总科功能更新。未知的关于MBL总科的蛋白质。TW9814,一个假设的MBL总科蛋白质,在结构上和功能上进行调查。的晶体结构二聚的TW9814,证明TW9814功能磷酸二酯酶(PDE)的存在二价金属离子如锰(II)或镍(II)。衬底bis(对硝基苯磷酸盐(bpNPP))显示的二聚作用的重要性TW9814 bpNPP-hydrolyzing活动和酶和之间的交互衬底。效率(k (cat) / km)在碱性条件下相比之下,其他pde。似乎是通过二硫键调节,这是一个功能,不存在其他MBL总科的成员。平台的功能特性其他假设的MBL蛋白或其他superfamilies .

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《Acta crystallographica. Section D, Structural biology》 |2022年第4期|532-541|共10页
作者
Heo Yunseok; Park Soo Bong; Jeon Ye EunYun Ji HyeJeong Bo GyeongCha Sun ShinLee Weontae;
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Dept Biochem,Yonsei Univ;

Dept Chem & Nanosci,Ewha Womans Univ;

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正文语种英语
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phosphodiesterase; crystal structure; superfamilyMBL3P genefamilyDisulfide LinkageEnzymes;

机译：磷酸二酯酶;水晶结构;superfamilyMBL3P genefamilyDisulfideLinkageEnzymes;

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Structural and functional identification of the uncharacterized metallo-beta-lactamase superfamily protein TW9814 as a phosphodiesterase with unique metal coordination

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