5XW2

Crystal structure of the Hydroxylase HmtN in C 1 2 1 crystal form

5XW2 の概要

• エントリーDOI: 10.2210/pdb5xw2/pdb
• 関連するPDBエントリー: 4E2P
• 分子名称: Cytochrome P450 107B1 (P450CVIIB1), PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: himastatin, hydroxylase, cytochrome p450, biosynthetic protein
• 由来する生物種: Streptomyces himastatinicus ATCC 53653
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48026.65

構造登録者

Zhang, H.D.,Zhang, H.J. (登録日: 2017-06-29, 公開日: 2018-04-25, 最終更新日: 2023-11-22)

主引用文献

Zhang, H.,Chen, J.,Zhang, H.
Molecular characterization of the hydroxylase HmtN at 1.3 angstrom resolution.
Biochem. Biophys. Res. Commun., 2017

PubMed Abstract: Himastatin is a novel antibiotic with antitumor and antibacterial activity. In the himastatin biosynthesis pathway, HmtN is responsible for the hydroxylation of the piperazic acid (Pip) motif. Herein, we present the crystal structures of HmtN (1.3 Å), which is the first structure for a cytochrome P450 involved in the hydroxylation of cyclohexadepsipeptide during himastatin biosynthesis. Structure analysis indicated that almost all the surface of HmtN has negative electrostatic potential, only small patches of positive electrostatic potential can be found. It is worth noting that almost the entire active site of HmtT is negatively charged, while HmtN active site is composed of positive and negative charge. This may be relevant to their specific substrate recognition and different catalytic function. In addition, three channels were observed in HmtN crystal structure; channel 3 may be essential for substrate ingress and egress from the active site to the surface, while channel 1 and channel 2 may be the solvent and water pathway, respectively.

PubMed: 28687492
DOI: 10.1016/j.bbrc.2017.07.010

実験手法

X-RAY DIFFRACTION (1.298 Å)