6MTG

A Single Reactive Noncanonical Amino Acid is Able to Dramatically Stabilize Protein Structure

6MTG の概要

• エントリーDOI: 10.2210/pdb6mtg/pdb
• 分子名称: Homoserine O-succinyltransferase, DI(HYDROXYETHYL)ETHER, FORMIC ACID, ... (5 entities in total)
• 機能のキーワード: noncanonical amino acid, isothiocyanate, crosslink, thiourea, stabilization, transferase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70703.12

構造登録者

Li, J.C.,Nasertorabi, F.,Xuan, W.,Han, G.W.,Stevens, R.C.,Schultz, P.G. (登録日: 2018-10-19, 公開日: 2019-06-26, 最終更新日: 2024-11-06)

主引用文献

Li, J.C.,Nastertorabi, F.,Xuan, W.,Han, G.W.,Stevens, R.C.,Schultz, P.G.
A Single Reactive Noncanonical Amino Acid Is Able to Dramatically Stabilize Protein Structure.
Acs Chem.Biol., 14:1150-1153, 2019

PubMed Abstract: A p-isothiocyanate phenylalanine mutant of the homodimeric protein homoserine o-succinyltransferase (MetA) was isolated in a temperature dependent selection from a library of metA mutants containing noncanonical amino acids. This mutant protein has a dramatic increase of 24 °C in thermal stability compared to the wild type protein. Peptide mapping experiments revealed that the isothiocyanate group forms a thiourea cross-link to the N terminal proline of the other monomer, despite the two positions being >30 Å apart in the X-ray crystal structure of the wild type protein. These results show that an expanded set of building blocks beyond the canonical 20 amino acids can lead to significant changes in the properties of proteins.

PubMed: 31181898
DOI: 10.1021/acschembio.9b00002

実験手法

X-RAY DIFFRACTION (1.85 Å)