4R84

Crystal structure of Sialyltransferase from Photobacterium damsela with CMP-3F(a)Neu5Ac bound

Summary for 4R84

• Entry DOI: 10.2210/pdb4r84/pdb
• Related: 4R83
• Descriptor: Sialyltransferase 0160, CYTIDINE-5'-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC ACID, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: rossmann fold, glycosyltransferase gt-b structural group, transferase
• Biological source: Photobacterium damselae
• Total number of polymer chains: 4
• Total formula weight: 230018.66

Authors

Fisher, A.J.,Chen, X.,Li, Y.,Huynh, N. (deposition date: 2014-08-29, release date: 2014-12-03, Last modification date: 2024-11-20)

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 (1.7 Å)