5TU4

PagF with Boc-Tyr and DMSPP

5TU4 の概要

• エントリーDOI: 10.2210/pdb5tu4/pdb
• 関連するPDBエントリー: 5TU5 5TU6 5TYY
• 分子名称: PagF prenyltransferase, DIMETHYLALLYL S-THIOLODIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: ripp, prenylation, abba fold, transferase
• 由来する生物種: Planktothrix agardhii NIES-596
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35792.74

構造登録者

Hao, Y.,Nair, S.K. (登録日: 2016-11-04, 公開日: 2016-11-30, 最終更新日: 2024-03-06)

主引用文献

Hao, Y.,Pierce, E.,Roe, D.,Morita, M.,McIntosh, J.A.,Agarwal, V.,Cheatham, T.E.,Schmidt, E.W.,Nair, S.K.
Molecular basis for the broad substrate selectivity of a peptide prenyltransferase.
Proc. Natl. Acad. Sci. U.S.A., 113:14037-14042, 2016

PubMed Abstract: The cyanobactin prenyltransferases catalyze a series of known or unprecedented reactions on millions of different substrates, with no easily observable recognition motif and exquisite regioselectivity. Here we define the basis of broad substrate tolerance for the otherwise uncharacterized TruF family. We determined the structures of the Tyr-prenylating enzyme PagF, in complex with an isoprenoid donor analog and a panel of linear and macrocyclic peptide substrates. Unexpectedly, the structures reveal a truncated barrel fold, wherein binding of large peptide substrates is necessary to complete a solvent-exposed hydrophobic pocket to form the catalytically competent active site. Kinetic, mutational, chemical, and computational analyses revealed the structural basis of selectivity, showing a small motif within peptide substrates that is sufficient for recognition by the enzyme. Attaching this 2-residue motif to two random peptides results in their isoprenylation by PagF, demonstrating utility as a general biocatalytic platform for modifications on any peptide substrate.

PubMed: 27872314
DOI: 10.1073/pnas.1609869113

実験手法

X-RAY DIFFRACTION (2.1 Å)