5Z0Q
Crystal Structure of OvoB
Summary for 5Z0Q
| Entry DOI | 10.2210/pdb5z0q/pdb |
| Descriptor | Aminotransferase, class I and II, PYRIDOXAL-5'-PHOSPHATE (2 entities in total) |
| Functional Keywords | ovothiol a, biosynthesis, c-s lyase, aminotransferase, plp coenzyme, biosynthetic protein, transferase |
| Biological source | Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99) |
| Total number of polymer chains | 12 |
| Total formula weight | 528551.88 |
| Authors | Cai, Y.J.,Huang, P.,Wu, L.,Zhou, J.H.,Liu, P.H. (deposition date: 2017-12-20, release date: 2018-11-07, Last modification date: 2023-11-22) |
| Primary citation | Naowarojna, N.,Huang, P.,Cai, Y.,Song, H.,Wu, L.,Cheng, R.,Li, Y.,Wang, S.,Lyu, H.,Zhang, L.,Zhou, J.,Liu, P. In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C-S Lyase and Methyltransferase Reactions. Org. Lett., 20:5427-5430, 2018 Cited by PubMed Abstract: Ovothiols are thiolhistidine derivatives. The first step of ovothiol biosynthesis is OvoA-catalyzed oxidative coupling between histidine and cysteine. In this report, the remaining steps of ovothiol A biosynthesis were reconstituted in vitro. ETA_14770 (OvoB) was reported as a PLP-dependent sulfoxide lyase, responsible for mercaptohistidine production. OvoA was found to be a bifunctional enzyme, which mediates both oxidative C-S bond formation and methylation of mercaptohistidine to afford ovothiol A. Besides reconstituting the whole biosynthetic pathway, two unique features proposed in the literature were also examined: a potential cysteine-recycling mechanism of the C-S lyase (OvoB) and the selectivity of the π- N methyltransferase. PubMed: 30141637DOI: 10.1021/acs.orglett.8b02332 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.77 Å) |
Structure validation
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