6i1r | pdb_00006i1r

Crystal structure of CMP bound CST in an outward facing conformation

spinqualitylabelsall models 6i1r, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i1r is a 2 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: C5P Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B4FZ94_MAIZE Publication Abstract from PubMed 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. Structural basis for the delivery of activated sialic acid into Golgi for sialyation.,Nji E, Gulati A, Qureshi AA, Coincon M, Drew D Nat Struct Mol Biol. 2019 May 27. pii: 10.1038/s41594-019-0225-y. doi:, 10.1038/s41594-019-0225-y. PMID:31133698 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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