Enzymology
Identification and Characterization of a Novel Prokaryotic Peptide: N-GLYCOSIDASE FROM ELIZABETHKINGIA MENINGOSEPTICA*

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Peptide:N-glycosidase (PNGase) F, the first PNGase identified in prokaryotic cells, catalyzes the removal of intact asparagine-linked oligosaccharide chains from glycoproteins and/or glycopeptides. Since its discovery in 1984, PNGase F has remained as the sole prokaryotic PNGase. Recently, a novel gene encoding a protein with a predicted PNGase domain was identified from a clinical isolate of Elizabethkingia meningoseptica. In this study, the candidate protein was expressed in vitro and was subjected to biochemical and structural analyses. The results revealed that it possesses PNGase activity and has substrate specificity different from that of PNGase F. The crystal structure of the protein was determined at 1.9 Å resolution. Structural comparison with PNGase F revealed a relatively larger glycan-binding groove in the catalytic domain and an additional bowl-like domain with unknown function at the N terminus of the candidate protein. These structural and functional analyses indicated that the candidate protein is a novel prokaryotic N-glycosidase. The protein has been named PNGase F-II.

Bacteria
Crystal Structure
Enzyme
Glycoprotein
N-Linked Glycosylation
Peptide:N-Glycosidase (PNGase), PNGase F, Glycosylation, Deglycosylation, Glycoprotein, Crystal Structure

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The atomic coordinates and structure factors (codes 4R4X and 4R4Z) have been deposited in the Protein Data Bank (http://wwpdb.org/).

*

This work was supported in part by Fudan University Grant EZF101507. A part of this work was performed under the National Science and Technology Major Project of China (2012ZX10003008-010). This work was also supported in part by Ministry of Science and Technology of China Grants 2012CB910502 and 2011CB966304.

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G. Sun and L. Chen, submitted for publication.

1

Both authors contributed equally to this work.

2

Both authors contributed equally to this work.