Structural insights into the substrate binding sites of O-carbamoyltransferase VtdB from Streptomyces sp. NO1W98.

The O-carbamoyltransferase VtdB catalyzes the carbamoylation of venturicidin B, which is essential for the biosynthesis of the antibiotic venturicidin A. Here, the crystal structures of VtdB and VtdB in complex with the intermediate carbamoyladenylate (VtdBCAO) were determined at resolutions of 2.99 Å and 2.90 Å, respectively. The structures resemble the conserved YrdC-like and specific Kae1-like domains. A magnesium ion and the intermediate carbamoyladenylate were also observed in the Kae1-like domain of VtdB. The structure of VtdBCAO in complex with the substrate venturicidin B was modeled by a molecular docking method to better understand the substrate binding mode, revealing a novel venturicidin B binding pocket. Copyright © 2023 Elsevier Inc. All rights reserved.

Citation

De-Fa Rao, Hui Zhang, Ju-Ling Wang, Xiao-Xiao Meng, Zhen-Zhen Li, Chun-Ya Xie, Ikrame El Jaidi, Li Dai, Jing-Jing Ye, Min Zhu, Yu-Jie Peng, Qi Chen, Dao-Xiang Zhang, Yan-Bin Teng. Structural insights into the substrate binding sites of O-carbamoyltransferase VtdB from Streptomyces sp. NO1W98. Biochemical and biophysical research communications. 2023 Jun 04;659:40-45

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PMID: 37031593

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