6I1Z
Outward facing structure of apo CST
Summary for 6I1Z
| Entry DOI | 10.2210/pdb6i1z/pdb |
| Related | 6I1R |
| Descriptor | CMP-sialic acid transporter 1 (1 entity in total) |
| Functional Keywords | cmp-sialic acid transporter, secondary active transporter, nucleotide sugar transporter, slc35a1, membrane protein |
| Biological source | Zea mays (Maize) |
| Total number of polymer chains | 2 |
| Total formula weight | 73037.96 |
| 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 citation | 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 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: 31133698DOI: 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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