6D6Z

Structure of the malate racemase apoprotein from Thermoanaerobacterium thermosaccharolyticum

6D6Z の概要

• エントリーDOI: 10.2210/pdb6d6z/pdb
• 分子名称: Malate racemase Mar2 (2 entities in total)
• 機能のキーワード: lar, lactate racemase, isomerase
• 由来する生物種: Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814) (Clostridium thermosaccharolyticum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47559.42

構造登録者

Fellner, M.,Hausinger, R.P.,Hu, J. (登録日: 2018-04-23, 公開日: 2019-04-24, 最終更新日: 2023-10-04)

主引用文献

Desguin, B.,Urdiain-Arraiza, J.,Da Costa, M.,Fellner, M.,Hu, J.,Hausinger, R.P.,Desmet, T.,Hols, P.,Soumillion, P.
Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases.
Sci Rep, 10:18123-18123, 2020

PubMed Abstract: Isomerization reactions are fundamental in biology. Lactate racemase, which isomerizes L- and D-lactate, is composed of the LarA protein and a nickel-containing cofactor, the nickel-pincer nucleotide (NPN). In this study, we show that LarA is part of a superfamily containing many different enzymes. We overexpressed and purified 13 lactate racemase homologs, incorporated the NPN cofactor, and assayed the isomerization of different substrates guided by gene context analysis. We discovered two malate racemases, one phenyllactate racemase, one α-hydroxyglutarate racemase, two D-gluconate 2-epimerases, and one short-chain aliphatic α-hydroxyacid racemase among the tested enzymes. We solved the structure of a malate racemase apoprotein and used it, along with the previously described structures of lactate racemase holoprotein and D-gluconate epimerase apoprotein, to identify key residues involved in substrate binding. This study demonstrates that the NPN cofactor is used by a diverse superfamily of α-hydroxyacid racemases and epimerases, widely expanding the scope of NPN-dependent enzymes.

PubMed: 33093595
DOI: 10.1038/s41598-020-74802-6

実験手法

X-RAY DIFFRACTION (2.38 Å)