4R9V

Crystal structure of sialyltransferase from photobacterium damselae, residues 113-497 corresponding to the gt-b domain

Summary for 4R9V

• Entry DOI: 10.2210/pdb4r9v/pdb
• Related: 4R83 4R84
• Descriptor: Sialyltransferase 0160, CALCIUM ION (3 entities in total)
• Functional Keywords: rossmann fold, glycosyltransferase gt-b structural group, transferase
• Biological source: Photobacterium damselae
• Total number of polymer chains: 1
• Total formula weight: 46195.65

Authors

Li, Y.,Huynh, N.,Chen, X.,Fisher, A.J. (deposition date: 2014-09-08, release date: 2014-12-03, Last modification date: 2023-09-20)

Primary citation

Huynh, N.,Li, Y.,Yu, H.,Huang, S.,Lau, K.,Chen, X.,Fisher, A.J.
Crystal structures of sialyltransferase from Photobacterium damselae.
Febs Lett., 588:4720-4729, 2014

PubMed Abstract: 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 α2-6-sialyltransferase has been used efficiently in enzymatic and chemoenzymatic synthesis of α2-6-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.

PubMed: 25451227
DOI: 10.1016/j.febslet.2014.11.003

Experimental method

X-RAY DIFFRACTION (2.3 Å)