5Z0Y

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

Summary for 5Z0Y

• Entry DOI: 10.2210/pdb5z0y/pdb
• Descriptor: Serine hydroxymethyltransferase, GLYCEROL (3 entities in total)
• Functional Keywords: shmt, pichia pastoris, cytoplasm serine hydroxymethyltransferase, transferase
• Biological source: Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1) (Yeast)
• Total number of polymer chains: 1
• Total formula weight: 52243.33

Authors

Chen, Z.,Zhang, M. (deposition date: 2017-12-22, release date: 2018-03-14, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)