Structural highlights
Publication Abstract from PubMed
Sialyltransferase structures fall into either GT-A or GT-B glycosyltransferase fold. Some sialyltransferases from the Photobacterium genus have been shown to contain an additional N-terminal immunoglobulin (Ig)-like domain. Photobacterium damselae alpha2-6-sialyltransferase has been used efficiently in enzymatic and chemoenzymatic synthesis of alpha2-6-linked sialosides. Here we report three crystal structures of this enzyme. Two structures with and without a donor substrate analog CMP-3F(a)Neu5Ac contain an immunoglobulin (Ig)-like domain and adopt the GT-B sialyltransferase fold. The binary structure reveals a non-productive pre-Michaelis complex, which are caused by crystal lattice contacts that prevent the large conformational changes. The third structure lacks the Ig-domain. Comparison of the three structures reveals small inherent flexibility between the two Rossmann-like domains of the GT-B fold.
Crystal structures of sialyltransferase from Photobacterium damselae.,Huynh N, Li Y, Yu H, Huang S, Lau K, Chen X, Fisher AJ FEBS Lett. 2014 Dec 20;588(24):4720-9. doi: 10.1016/j.febslet.2014.11.003. Epub, 2014 Nov 15. PMID:25451227[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huynh N, Li Y, Yu H, Huang S, Lau K, Chen X, Fisher AJ. Crystal structures of sialyltransferase from Photobacterium damselae. FEBS Lett. 2014 Dec 20;588(24):4720-9. doi: 10.1016/j.febslet.2014.11.003. Epub, 2014 Nov 15. PMID:25451227 doi:http://dx.doi.org/10.1016/j.febslet.2014.11.003
