8g8k | pdb_00008g8k

Crystal structure of Rv1916 (residues 233-398)

spinqualitylabelsall models 8g8k, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8g8k is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.54Å Ligands: EDO, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACEAB_MYCTU Together with AceAa, they could catalyze the formation of succinate and glyoxylate from isocitrate. Publication Abstract from PubMed 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 (1) 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. Mycobacterium tuberculosis Rv1916 is an Acetyl-CoA-Binding Protein.,Huang EY, Kwai BXC, Bhusal RP, Bashiri G, Leung IKH Chembiochem. 2023 Jul 17;24(14):e202300162. doi: 10.1002/cbic.202300162. Epub , 2023 Jun 18. PMID:37211532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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