YcaO

YcaO-like family

Structure of the heterocyclase TruD. A YcaO-like protein from Prochloron sp. 06037A PDB entry 4bs9[1]
Identifiers
Symbol YcaO
Pfam PF02624
InterPro IPR003776

YcaO is a protein found in bacteria which is involved in the synthesis of thiazole/oxazole modified microcin antibiotics, such as bottromycin. YcaO performs ATP dependent cylodehydration to form the oxazole and thiazole moieties of the microcin.[2][3][4]

References

  1. Koehnke, J.; Bent, A. F.; Zollman, D.; Smith, K.; Houssen, W. E.; Zhu, X.; Mann, G.; Lebl, T.; Scharff, R.; Shirran, S.; Botting, C. H.; Jaspars, M.; Schwarz-Linek, U.; Naismith, J. H. (2013). "The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction". Angewandte Chemie International Edition 52 (52): 13991–13996. doi:10.1002/anie.201306302. PMC 3995012. PMID 24214017.
  2. Dunbar, K. L.; Melby, J. O.; Mitchell, D. A. (2012). "YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations". Nature Chemical Biology 8 (6): 569–575. doi:10.1038/nchembio.944. PMC 3428213. PMID 22522320.
  3. Dunbar KL, Chekan JR, Cox CL, Burkhart BJ, Nair SK, Mitchell DA (2014). "Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis". Nature Chemical Biology 10 (10): 823–9. doi:10.1038/nchembio.1608. PMC 4167974. PMID 25129028.
  4. Koehnke J, Mann G, Bent AF, Ludewig H, Shirran S, Botting C, Lebl T, Houssen WE, Jaspars M, Naismith JH (2015). "Structural analysis of leader peptide binding enables leader-free cyanobactin processing". Nature Chemical Biology 11: 558–63. doi:10.1038/nchembio.1841. PMID 26098679.


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