5Z0Y

Crystallization and structure determination of cytoplasm serine hydroxymethyltransferase (SHMT) from Pichia pastoris

5Z0Y の概要

• エントリーDOI: 10.2210/pdb5z0y/pdb
• 分子名称: Serine hydroxymethyltransferase, GLYCEROL (3 entities in total)
• 機能のキーワード: shmt, pichia pastoris, cytoplasm serine hydroxymethyltransferase, transferase
• 由来する生物種: Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1) (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52243.33

構造登録者

Chen, Z.,Zhang, M. (登録日: 2017-12-22, 公開日: 2018-03-14, 最終更新日: 2023-11-22)

主引用文献

Zhang, M.,Wu, W.,Chen, Z.
Structure and function of cytoplasmic serine hydroxymethyltransferase from Pichia pastoris
Biochem. Biophys. Res. Commun., 496:753-757, 2018

PubMed Abstract: Serine hydroxymethyltransferase (SHMT) catalyzes the interconversion of serine and glycine, which is crucial for one carbon metabolism. Here, we report the first crystal structure of cytoplasmic SHMT from Pichia pastoris (pcSHMT) diffracted to 2.5 Å resolution in space group C222. PcSHMT was a contaminant with our target protein expressed in Pichia pastoris and confirmed by mass spectrometry. The overall structure of pcSHMT is similar to Human mitochondrial SHMT and different to E. coli SHMT. Interestingly, the oligomerization of pcSHMT expressed in eukaryotic or prokaryotic system differs significantly and is regulated by pyridoxal-5'-phosphate. Our results revealed a close evolutionary relationship between Pichia pastoris and Human mitochondria.

PubMed: 29339156
DOI: 10.1016/j.bbrc.2018.01.084

実験手法

X-RAY DIFFRACTION (2.5 Å)