6K5E

Crystal structure of BioH from Klebsiella pneumonia

6K5E の概要

• エントリーDOI: 10.2210/pdb6k5e/pdb
• 分子名称: Pimeloyl-[acyl-carrier protein] methyl ester esterase (2 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 169744.15

構造登録者

Wang, L.,Chen, Y. (登録日: 2019-05-28, 公開日: 2019-07-17, 最終更新日: 2024-11-20)

主引用文献

Wang, L.,Chen, Y.,Shang, F.,Liu, W.,Lan, J.,Gao, P.,Ha, N.C.,Nam, K.H.,Dong, Y.,Quan, C.,Xu, Y.
Structural insight into the carboxylesterase BioH from Klebsiella pneumoniae.
Biochem.Biophys.Res.Commun., 520:538-543, 2019

PubMed Abstract: The BioH carboxylesterase which is a typical α/β-hydrolase enzyme involved in biotin synthetic pathway in most bacteria. BioH acts as a gatekeeper and blocks the further elongation of its substrate. In the pathogen Klebsiella pneumoniae, BioH plays a critical role in the biosynthesis of biotin. To better understand the molecular function of BioH, we determined the crystal structure of BioH from K. pneumoniae at 2.26 Å resolution using X-ray crystallography. The structure of KpBioH consists of an α-β-α sandwich domain and a cap domain. B-factor analysis revealed that the α-β-α sandwich domain is a rigid structure, while the loops in the cap domain shows the structural flexibility. The active site of KpBioH contains the catalytic triad (Ser82-Asp207-His235) on the interface of the α-β-α sandwich domain, which is surrounded by the cap domain. Size exclusion chromatography shows that KpBioH prefers the monomeric state in solution, whereas two-fold symmetric dimeric formation of KpBioH was observed in the asymmetric unit, the conserved Cys31-based disulfide bonds can maintain the irreversible dimeric formation of KpBioH. Our study provides important structural insight for understanding the molecular mechanisms of KpBioH and its homologous proteins.

PubMed: 31615653
DOI: 10.1016/j.bbrc.2019.10.050

実験手法

X-RAY DIFFRACTION (2.257 Å)