Article Metrics


Online attention

Structural basis for the delivery of activated sialic acid into Golgi for sialyation

DOI: 10.1038/s41594-019-0225-y DOI Help

Authors: Emmanuel Nji (Stockholm University) , Ashutosh Gulati (Stockholm University) , Abdul Aziz Qureshi (Stockholm University) , Mathieu Coincon (Stockholm University) , David Drew (Stockholm University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology , VOL 14

State: Published (Approved)
Published: May 2019

Abstract: The decoration of secretory glycoproteins and glycolipids with sialic acid is critical to many physiological and pathological processes. Sialyation is dependent on a continuous supply of sialic acid into Golgi organelles in the form of CMP-sialic acid. Translocation of CMP-sialic acid into Golgi is carried out by the CMP-sialic acid transporter (CST). Mutations in human CST are linked to glycosylation disorders, and CST is important for glycopathway engineering, as it is critical for sialyation efficiency of therapeutic glycoproteins. The mechanism of how CMP-sialic acid is recognized and translocated across Golgi membranes in exchange for CMP is poorly understood. Here we have determined the crystal structure of a Zea mays CST in complex with CMP. We conclude that the specificity of CST for CMP-sialic acid is established by the recognition of the nucleotide CMP to such an extent that they are mechanistically capable of both passive and coupled antiporter activity.

Journal Keywords: Diseases; Glycobiology; Golgi; Membrane proteins; X-ray crystallography

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I03-Macromolecular Crystallography

Other Facilities: ESRF

Added On: 03/06/2019 15:40

Discipline Tags:

Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)