8KIF

The structure of MmaE with substrate

8KIF の概要

• エントリーDOI: 10.2210/pdb8kif/pdb
• 分子名称: Putative dioxygenase, FE (II) ION, (3R)-3-(2-hydroxy-2-oxoethylamino)decanoic acid, ... (4 entities in total)
• 機能のキーワード: mmae, fe/2og enzymes, oxidoreductase
• 由来する生物種: Mycobacterium marinum M
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 137635.23

構造登録者

Chen, J.,Zhou, J. (登録日: 2023-08-23, 公開日: 2024-04-17, 最終更新日: 2025-07-16)

主引用文献

Chen, T.Y.,Chen, J.,Ruszczycky, M.W.,Hilovsky, D.,Hostetler, T.,Liu, X.,Zhou, J.,Chang, W.C.
Variation in biosynthesis and metal-binding properties of isonitrile-containing peptides produced by Mycobacteria versus Streptomyces.
Acs Catalysis, 14:4975-4983, 2024

PubMed Abstract: A number of bacteria are known to produce isonitrile-containing peptides (INPs) that facilitate metal transport and are important for cell survival; however, considerable structural variation is observed among INPs depending on the producing organism. While non-heme iron 2-oxoglutarate dependent isonitrilases catalyze isonitrile formation, how the natural variation in INP structure is controlled and its implications for INP bioactivity remain open questions. Herein, total chemical synthesis is utilized with X-Ray crystallographic analysis of mycobacterial isonitrilases to provide a structural model of substrate specificity that explains the longer alkyl chains observed in mycobacterial versus Streptomyces INPs. Moreover, proton NMR titration experiments demonstrate that INPs regardless of alkyl chain length are specific for binding copper instead of zinc. These results suggest that isonitrilases may act as gatekeepers in modulating the observed biological distribution of INP structures and this distribution may be primarily related to differing metal transport requirements among the producing strains.

PubMed: 38895101
DOI: 10.1021/acscatal.4c00645

実験手法

X-RAY DIFFRACTION (2.13 Å)