8SY2

Peanut USP-type BURP Domain Peptide Cyclase

8SY2 の概要

• エントリーDOI: 10.2210/pdb8sy2/pdb
• 関連するPDBエントリー: 8SY3
• 分子名称: BURP domain-containing protein (2 entities in total)
• 機能のキーワード: unliganded, oxidoreductase
• 由来する生物種: Arachis hypogaea (peanut)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57571.67

構造登録者

Mydy, L.S.,Kersten, R.D.,Smith, J.L. (登録日: 2023-05-24, 公開日: 2024-02-14, 最終更新日: 2024-10-16)

主引用文献

Mydy, L.S.,Hungerford, J.,Chigumba, D.N.,Konwerski, J.R.,Jantzi, S.C.,Wang, D.,Smith, J.L.,Kersten, R.D.
An intramolecular macrocyclase in plant ribosomal peptide biosynthesis.
Nat.Chem.Biol., 20:530-540, 2024

PubMed Abstract: The biosynthetic dogma of ribosomally synthesized and posttranslationally modified peptides (RiPP) involves enzymatic intermolecular modification of core peptide motifs in precursor peptides. The plant-specific BURP-domain protein family, named after their four founding members, includes autocatalytic peptide cyclases involved in the biosynthesis of side-chain-macrocyclic plant RiPPs. Here we show that AhyBURP, a representative of the founding Unknown Seed Protein-type BURP-domain subfamily, catalyzes intramolecular macrocyclizations of its core peptide during the sequential biosynthesis of monocyclic lyciumin I via glycine-tryptophan crosslinking and bicyclic legumenin via glutamine-tyrosine crosslinking. X-ray crystallography of AhyBURP reveals the BURP-domain fold with two type II copper centers derived from a conserved stapled-disulfide and His motif. We show the macrocyclization of lyciumin-C(sp)-N-bond formation followed by legumenin-C(sp)-O-bond formation requires dioxygen and radical involvement based on enzyme assays in anoxic conditions and isotopic labeling. Our study expands enzymatic intramolecular modifications beyond catalytic moiety and chromophore biogenesis to RiPP biosynthesis.

PubMed: 38355722
DOI: 10.1038/s41589-024-01552-1

実験手法

X-RAY DIFFRACTION (2.67 Å)