6I1R

Crystal structure of CMP bound CST in an outward facing conformation

6I1R の概要

• エントリーDOI: 10.2210/pdb6i1r/pdb
• 分子名称: CMP-sialic acid transporter 1, CYTIDINE-5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: cmp-sialic acid transporter, secondary active transporter, nucleotide sugar transporter, slc35a1, membrane protein
• 由来する生物種: Zea mays (Maize)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73684.35

構造登録者

Nji, E.,Gulati, A.,Qureshi, A.A.,Drew, D. (登録日: 2018-10-30, 公開日: 2019-06-05, 最終更新日: 2024-01-24)

主引用文献

Nji, 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

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

実験手法

X-RAY DIFFRACTION (2.8 Å)