4V1T

Heterocyclase in complex with substrate and Cofactor

4V1T の概要

• エントリーDOI: 10.2210/pdb4v1t/pdb
• 関連するPDBエントリー: 4V1U 4V1V
• 分子名称: LYND, PATE, ZINC ION, ... (7 entities in total)
• 機能のキーワード: hydrolase, cyanobactins
• 由来する生物種: LYNGBYA AESTUARII; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 187547.40

構造登録者

Koehnke, J.,Naismith, J.H. (登録日: 2014-10-02, 公開日: 2015-01-14, 最終更新日: 2024-05-08)

主引用文献

Koehnke, J.,Mann, G.,Bent, A.F.,Ludewig, H.,Shirran, S.,Botting, C.,Lebl, T.,Houssen, W.,Jaspars, M.,Naismith, J.H.
Structural Analysis of Leader Peptide Binding Enables Leader-Free Cyanobactin Processing
Nat.Chem.Biol., 11:558-, 2015

PubMed Abstract: Regioselective modification of amino acids within the context of a peptide is common to a number of biosynthetic pathways, and many of the resulting products have potential as therapeutics. The ATP-dependent enzyme LynD heterocyclizes multiple cysteine residues to thiazolines within a peptide substrate. The enzyme requires the substrate to have a conserved N-terminal leader for full activity. Catalysis is almost insensitive to immediately flanking residues in the substrate, suggesting that recognition occurs distant from the active site. Nucleotide and peptide substrate co-complex structures of LynD reveal that the substrate leader peptide binds to and extends the β-sheet of a conserved domain of LynD, whereas catalysis is accomplished in another conserved domain. The spatial segregation of catalysis from recognition combines seemingly contradictory properties of regioselectivity and promiscuity, and it appears to be a conserved strategy in other peptide-modifying enzymes. A variant of LynD that efficiently processes substrates without a leader peptide has been engineered.

PubMed: 26098679
DOI: 10.1038/NCHEMBIO.1841

実験手法

X-RAY DIFFRACTION (2.14 Å)