화학공학소재연구정보센터
Biochemical and Biophysical Research Communications, Vol.496, No.2, 753-757, 2018
Structure and function of cytoplasmic serine hydroxymethyltransferase from Pichia pastoris
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 angstrom resolution in space group C222(1). 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 mitochondria! 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. (C) 2018 Elsevier Inc. All rights reserved.