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6I1Z

Outward facing structure of apo CST

Summary for 6I1Z
Entry DOI10.2210/pdb6i1z/pdb
Related6I1R
DescriptorCMP-sialic acid transporter 1 (1 entity in total)
Functional Keywordscmp-sialic acid transporter, secondary active transporter, nucleotide sugar transporter, slc35a1, membrane protein
Biological sourceZea mays (Maize)
Total number of polymer chains2
Total formula weight73037.96
Authors
Nji, E.,Gulati, A.,Qureshi, A.A.,Drew, D. (deposition date: 2018-10-31, release date: 2019-06-05, Last modification date: 2024-01-24)
Primary citationNji, E.,Gulati, A.,Qureshi, A.A.,Coincon, M.,Drew, D.
Structural basis for the delivery of activated sialic acid into Golgi for sialyation.
Nat.Struct.Mol.Biol., 26:415-423, 2019
Cited by
PubMed 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.
PubMed: 31133698
DOI: 10.1038/s41594-019-0225-y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

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