9SOV の概要
| エントリーDOI | 10.2210/pdb9sov/pdb |
| 分子名称 | Methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, (7~{S},10~{S},13~{S})-13-(methylamino)-10-(2-methylpropyl)-18-oxidanyl-9,12-bis(oxidanylidene)-2,4,8,11-tetrazatricyclo[13.3.1.1^{2,5}]icosa-1(19),3,5(20),15,17-pentaene-7-carboxylic acid, ... (4 entities in total) |
| 機能のキーワード | corz in complex with sah, methyltransferase and myxarylin, myxarylin methyltransferase, biosynthetic protein |
| 由来する生物種 | Corallococcus coralloides |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 96610.74 |
| 構造登録者 | |
| 主引用文献 | Sikandar, A.,Vianey, L.,Schliessmann, K.,Shen, Q.,Mackay, C.L.,Haeckl, F.P.J.,Urlacher, V.B.,Naismith, J.H.,Muller, R. Myxarylin: Total In Vitro Biosynthesis, Expansion of Substrate Scope, and Bioengineered Thioamidated Biarylitides. J.Am.Chem.Soc., 148:6970-6980, 2026 Cited by PubMed Abstract: Biarylitides are a new class of ribosomally synthesized and post-translationally modified peptides (RiPPs) featuring the smallest reported precursor peptide and cytochrome P450-mediated cross-links. Here, we report the complete reconstitution of the myxobacterial biarylitide, myxarylin. We demonstrate that cross-linking is the first step and acts as a gatekeeper for downstream processing. The cytochrome P450 enzyme P450 from the myxarylin biosynthetic gene cluster exhibits remarkable substrate tolerance, allowing biosynthesis of new-to-nature thioamidated biarylitides through an unprecedented modular precursor peptide engineering approach. Surprisingly, changes in the precursor peptide sequence resulted in a shift in the installation of the P450-mediated modification from the expected C- to the N-terminus. Leader peptide removal follows cross-linking and is likely carried out by a prolyl oligopeptidase (POP), a member of the serine protease family. The last step of the pathway involves N-terminal methylation, which also prevents premature degradation of the pathway intermediates by the POP. The crystal structure of the methyltransferase in complex with SAH and myxarylin allowed us to rationalize its substrate selectivity and guide protein engineering to expand its substrate scope. PubMed: 41687121DOI: 10.1021/jacs.5c17257 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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