5UNM

LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, substrate free form with flexible loop

5UNM の概要

• エントリーDOI: 10.2210/pdb5unm/pdb
• 分子名称: ATP-utilizing enzyme of the PP-loopsuperfamily, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: lar, sulfur transferase, lare, ampylation, hexamer, trimer, pp-loop, atp pyrophophatase domain, lactate, 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: 190882.42

構造登録者

Fellner, M.,Desguin, B.,Hausinger, R.P.,Hu, J. (登録日: 2017-01-31, 公開日: 2017-08-23, 最終更新日: 2024-03-06)

主引用文献

Fellner, M.,Desguin, B.,Hausinger, R.P.,Hu, J.
Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Proc. Natl. Acad. Sci. U.S.A., 114:9074-9079, 2017

PubMed Abstract: The operon in encodes five Lar proteins (LarA/B/C/D/E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. Previous studies have established that two molecules of LarE catalyze successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. However, the catalytic mechanism of this very unusual sulfur-sacrificing reaction remains elusive. In this work, we present the crystal structures of LarE in ligand-free and several ligand-bound forms, demonstrating that LarE is a member of the N-type ATP pyrophosphatase (PPase) family with a conserved N-terminal ATP PPase domain and a unique C-terminal domain harboring the putative catalytic site. Structural analysis, combined with structure-guided mutagenesis, leads us to propose a catalytic mechanism that establishes LarE as a paradigm for sulfur transfer through sacrificing its catalytic cysteine residue.

PubMed: 28784764
DOI: 10.1073/pnas.1704967114

実験手法

X-RAY DIFFRACTION (2.58 Å)