8HFD

Crystal structure of allantoinase from E. coli BL21

8HFD の概要

• エントリーDOI: 10.2210/pdb8hfd/pdb
• 分子名称: Allantoinase, DI(HYDROXYETHYL)ETHER, ZINC ION, ... (4 entities in total)
• 機能のキーワード: allantoinase, allantoin, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 203401.21

構造登録者

Lin, E.S.,Huang, H.Y.,Yang, P.C.,Liu, H.W.,Huang, C.Y. (登録日: 2022-11-10, 公開日: 2023-10-18, 最終更新日: 2023-11-15)

主引用文献

Huang, Y.H.,Yang, P.C.,Lin, E.S.,Ho, Y.Y.,Peng, W.F.,Lu, H.P.,Huang, C.C.,Huang, C.Y.
Crystal Structure of Allantoinase from Escherichia coli BL21: A Molecular Insight into a Role of the Active Site Loops in Catalysis.
Molecules, 28:-, 2023

PubMed Abstract: Allantoinase (ALLase; EC 3.5.2.5) possesses a binuclear metal center in which two metal ions are bridged by a posttranslationally carbamylated lysine. ALLase acts as a key enzyme for the biogenesis and degradation of ureides by catalyzing the conversion of allantoin into allantoate. Biochemically, ALLase belongs to the cyclic amidohydrolase family, which also includes dihydropyrimidinase, dihydroorotase, hydantoinase (HYDase), and imidase. Previously, the crystal structure of ALLase from K-12 (EcALLase-K12) was reported; however, the two active site loops crucial for substrate binding were not determined. This situation would limit further docking and protein engineering experiments. Here, we solved the crystal structure of BL21 ALLase (EcALLase-BL21) at a resolution of 2.07 Å (PDB ID 8HFD) to obtain more information for structural analyses. The structure has a classic TIM barrel fold. As compared with the previous work, the two missed active site loops in EcALLase-K12 were clearly determined in our structure of EcALLase-BL21. EcALLase-BL21 shared active site similarity with HYDase, an important biocatalyst for industrial production of semisynthetic penicillin and cephalosporins. Based on this structural comparison, we discussed the functional role of the two active site loops in EcALLase-BL21 to better understand the substrate/inhibitor binding mechanism for further biotechnological and pharmaceutical applications.

PubMed: 36677881
DOI: 10.3390/molecules28020827

実験手法

X-RAY DIFFRACTION (2.07 Å)