8G8K

Crystal structure of Rv1916 (residues 233-398)

8G8K の概要

• エントリーDOI: 10.2210/pdb8g8k/pdb
• 分子名称: Putative isocitrate lyase subunit B, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: isocitrate lyase, tuberculosis, biosynthetic protein
• 由来する生物種: Mycobacterium tuberculosis H37Rv
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19267.24

構造登録者

Kwai, B.X.C.,Bashiri, G.,Leung, I.K.H. (登録日: 2023-02-18, 公開日: 2023-06-07, 最終更新日: 2024-05-22)

主引用文献

Huang, E.Y.,Kwai, B.X.C.,Bhusal, R.P.,Bashiri, G.,Leung, I.K.H.
Mycobacterium tuberculosis Rv1916 is an Acetyl-CoA-Binding Protein.
Chembiochem, 24:e202300162-e202300162, 2023

PubMed Abstract: Isocitrate lyase (ICL) isoform 2 is an essential enzyme for some clinical Mycobacterium tuberculosis (Mtb) strains during infection. In the laboratory Mtb strain H37Rv, the icl2 gene encodes two distinct gene products - Rv1915 and Rv1916 - due to a frameshift mutation. This study aims to characterise these two gene products to understand their structure and function. While we were unable to produce Rv1915 recombinantly, soluble Rv1916 was obtained with sufficient yield for characterisation. Kinetic studies using UV-visible spectrophotometry and H-NMR spectroscopy showed that recombinant Rv1916 does not possess isocitrate lyase activity, while waterLOGSY binding experiments demonstrated that it could bind acetyl-CoA. Finally, X-ray crystallography revealed structural similarities between Rv1916 and the C-terminal domain of ICL2. Considering the probable differences between full-length ICL2 and the gene products Rv1915 and Rv1916, care must be taken when using Mtb H37Rv as a model organism to study central carbon metabolism.

PubMed: 37211532
DOI: 10.1002/cbic.202300162

実験手法

X-RAY DIFFRACTION (1.54 Å)