8KIF

The structure of MmaE with substrate

Summary for 8KIF

• Entry DOI: 10.2210/pdb8kif/pdb
• Descriptor: Putative dioxygenase, FE (II) ION, (3R)-3-(2-hydroxy-2-oxoethylamino)decanoic acid, ... (4 entities in total)
• Functional Keywords: mmae, fe/2og enzymes, oxidoreductase
• Biological source: Mycobacterium marinum M
• Total number of polymer chains: 4
• Total formula weight: 137635.23

Authors

Chen, J.,Zhou, J. (deposition date: 2023-08-23, release date: 2024-04-17, Last modification date: 2024-07-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.13 Å)