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Structure and Dynamics of N-Glycosylated Human Ribonuclease 1.

Abstract：

:Glycosylation is a common modification that can endow proteins with altered physical and biological properties. Ribonuclease 1 (RNase 1), which is the human homologue of the archetypal enzyme RNase A, undergoes N-linked glycosylation at asparagine residues 34, 76, and 88. We have produced the three individual glycoforms that display the core heptasaccharide, Man5GlcNAc2, and analyzed the structure of each glycoform by using small-angle X-ray scattering along with molecular dynamics simulations. The glycan on Asn34 is relatively compact and rigid, donates hydrogen bonds that "cap" the carbonyl groups at the C-terminus of an α-helix, and enhances protein thermostability. In contrast, the glycan on Asn88 is flexible and can even enter the enzymic active site, hindering catalysis. The N-glycosylation of Asn76 has less pronounced consequences. These data highlight the diverse behaviors of Man5GlcNAc2 pendants and provide a structural underpinning to the functional consequences of protein glycosylation.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Kilgore HR,Latham AP,Ressler VT,Zhang B,Raines RT

doi

10.1021/acs.biochem.0c00191

subject

Has Abstract

pub_date

2020-09-01 00:00:00

pages

3148-3156

issue

34

eissn

0006-2960

issn

1520-4995

journal_volume

59

pub_type

杂志文章

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