6UTT

LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with calcium

6UTT の概要

• エントリーDOI: 10.2210/pdb6utt/pdb
• 分子名称: ATP-dependent sacrificial sulfur transferase LarE, PHOSPHATE ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: lar, sulfur transferase, lare, ampylation, pp-loop, atp pyrophophatase domain, lactate racemization, lactate racemase, transferase
• 由来する生物種: Lactobacillus plantarum
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 191538.96

構造登録者

Fellner, M.,Huizenga, K.,Hausinger, R.P.,Hu, J. (登録日: 2019-10-29, 公開日: 2019-11-06, 最終更新日: 2023-10-11)

主引用文献

Fellner, M.,Huizenga, K.G.,Hausinger, R.P.,Hu, J.
Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Sci Rep, 10:5830-5830, 2020

PubMed Abstract: Detailed crystallographic characterization of a tri-aspartate metal-binding site previously identified on the three-fold symmetry axis of a hexameric enzyme, LarE from Lactobacillus plantarum, was conducted. By screening an array of monovalent, divalent, and trivalent metal ions, we demonstrated that this metal binding site stoichiometrically binds Ca, Mn, Fe/Fe, Co, Ni, Cu, Zn, and Cd, but not monovalent metal ions, Cr, Mg, Y, Sr or Ba. Extensive database searches resulted in only 13 similar metal binding sites in other proteins, indicative of the rareness of tri-aspartate architectures, which allows for engineering such a selective multivalent metal ion binding site into target macromolecules for structural and biophysical characterization.

PubMed: 32242052
DOI: 10.1038/s41598-020-62847-6

実験手法

X-RAY DIFFRACTION (2.49 Å)