Structural highlights
Function
SIAP_VIBCH Part of the tripartite ATP-independent periplasmic (TRAP) transport system SiaPQM that catalyzes unidirectional Na(+)-dependent sialic acid uptake. Binds the common sialic acid N-acetylneuraminic acid (Neu5Ac) with a high affinity.[1] [2]
References
- ↑ Mulligan C, Leech AP, Kelly DJ, Thomas GH. The membrane proteins SiaQ and SiaM form an essential stoichiometric complex in the sialic acid tripartite ATP-independent periplasmic (TRAP) transporter SiaPQM (VC1777-1779) from Vibrio cholerae. J Biol Chem. 2012 Jan 27;287(5):3598-608. doi: 10.1074/jbc.M111.281030. Epub 2011, Dec 13. PMID:22167185 doi:http://dx.doi.org/10.1074/jbc.M111.281030
- ↑ Chowdhury N, Norris J, McAlister E, Lau SYK, Thomas GH, Boyd EF. The VC1777-VC1779 proteins are members of a sialic acid-specific subfamily of TRAP transporters (SiaPQM) and constitute the sole route of sialic acid uptake in the human pathogen Vibrio cholerae. Microbiology (Reading). 2012 Aug;158(Pt 8):2158-2167. doi:, 10.1099/mic.0.059659-0. Epub 2012 May 3. PMID:22556361 doi:http://dx.doi.org/10.1099/mic.0.059659-0
