4GGV

Crystal Structure of HmtT Involved in Himastatin Biosynthesis

4GGV の概要

• エントリーDOI: 10.2210/pdb4ggv/pdb
• 分子名称: Cytochrome P450 superfamily protein, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: cysteine-ligand loop, hydrolase, oxidoreductase
• 由来する生物種: Streptomyces himastatinicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47093.98

構造登録者

Zhang, H.,Chen, J.,Wang, H.,Zhang, H. (登録日: 2012-08-07, 公開日: 2013-07-17, 最終更新日: 2023-11-08)

主引用文献

Zhang, H.,Chen, J.,Wang, H.,Xie, Y.,Ju, J.,Yan, Y.,Zhang, H.
Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis
Febs Lett., 587:1675-1680, 2013

PubMed Abstract: Himastatin is a novel antibiotic featuring a bicyclohexadepsipeptide structure. On the himastatin biosynthesis pathway, three cytochrome P450s (HmtT, HmtN, HmtS) are responsible for the post-tailoring of the cyclohexadepsipeptide backbone. Here we report the crystal structures of HmtT and HmtN. The overall structures of these two proteins are homologous to other cytochrome P450s. However, the exceptionally long F-G loop in HmtT has a highly unusual conformation and extends deep into the active site. As a result, the F/G helices of HmtT are both kinked. In contrast, the F/G helices of HmtN are straight. Also, the F/G helices in HmtT and HmtN take distinctive orientations, which may be a contributing factor for the substrate specificity of these two enzymes.

PubMed: 23611984
DOI: 10.1016/j.febslet.2013.04.013

実験手法

X-RAY DIFFRACTION (2.331 Å)