6GRI
E. coli Microcin synthetase McbBCD complex
6GRI の概要
エントリーDOI | 10.2210/pdb6gri/pdb |
分子名称 | Microcin B17-processing protein McbB, Microcin B17-processing protein McbC, Microcin B17-processing protein McbD, ... (8 entities in total) |
機能のキーワード | microcin, dna gyrase, heterocyclization, posttranslational modification, biosynthetic protein |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 144703.40 |
構造登録者 | Ghilarov, D.,Stevenson, C.E.M.,Travin, D.Y.,Piskunova, J.,Serebryakova, M.,Maxwell, A.,Lawson, D.M.,Severinov, K. (登録日: 2018-06-11, 公開日: 2019-01-30, 最終更新日: 2024-01-17) |
主引用文献 | Ghilarov, D.,Stevenson, C.E.M.,Travin, D.Y.,Piskunova, J.,Serebryakova, M.,Maxwell, A.,Lawson, D.M.,Severinov, K. Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting a Ribosomally Synthesized Peptide into a DNA Gyrase Poison. Mol. Cell, 73:749-762.e5, 2019 Cited by PubMed Abstract: The introduction of azole heterocycles into a peptide backbone is the principal step in the biosynthesis of numerous compounds with therapeutic potential. One of them is microcin B17, a bacterial topoisomerase inhibitor whose activity depends on the conversion of selected serine and cysteine residues of the precursor peptide to oxazoles and thiazoles by the McbBCD synthetase complex. Crystal structures of McbBCD reveal an octameric BCD complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer. An atomic-level view of the azole synthetase is a starting point for deeper understanding and control of biosynthesis of a large group of ribosomally synthesized natural products. PubMed: 30661981DOI: 10.1016/j.molcel.2018.11.032 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
構造検証レポート
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