5AX7

yeast pyruvyltransferase Pvg1p

Summary for 5AX7

• Entry DOI: 10.2210/pdb5ax7/pdb
• Descriptor: Pyruvyl transferase 1, ZINC ION (3 entities in total)
• Functional Keywords: pyruvylation, transferase
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• Total number of polymer chains: 2
• Total formula weight: 78276.85

Authors

Kanekiyo, M.,Yoritsune, K.,Yoshinaga, S.,Higuchi, Y.,Takegawa, K.,Kakuta, Y. (deposition date: 2015-07-16, release date: 2016-06-08, Last modification date: 2024-11-13)

Primary citation

Higuchi, Y.,Yoshinaga, S.,Yoritsune, K.,Tateno, H.,Hirabayashi, J.,Nakakita, S.,Kanekiyo, M.,Kakuta, Y.,Takegawa, K.
A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide
Sci Rep, 6:26349-26349, 2016

PubMed Abstract: Pyruvylation onto the terminus of oligosaccharide, widely seen from prokaryote to eukaryote, confers negative charges on the cell surface and seems to be functionally similar to sialylation, which is found at the end of human-type complex oligosaccharide. However, detailed molecular mechanisms underlying pyruvylation have not been clarified well. Here, we first determined the crystal structure of fission yeast pyruvyltransferase Pvg1p at a resolution of 2.46 Å. Subsequently, by combining molecular modeling with mutational analysis of active site residues, we obtained a Pvg1p mutant (Pvg1p(H168C)) that efficiently transferred pyruvyl moiety onto a human-type complex glycopeptide. The resultant pyruvylated human-type complex glycopeptide recognized similar lectins on lectin arrays as the α2,6-sialyl glycopeptides. This newly-generated pyruvylation of human-type complex oligosaccharides would provide a novel method for glyco-bioengineering.

PubMed: 27194449
DOI: 10.1038/srep26349

Experimental method

X-RAY DIFFRACTION (2.46 Å)