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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4720-4729 |
| Number of pages | 10 |
| Journal | FEBS Letters |
| Volume | 588 |
| Issue number | 24 |
| DOIs | |
| State | Published - Dec 20 2014 |
Fingerprint
Keywords
- CMP-3F(a)Neu5Ac
- Photobacterium damselae
- Protein crystal structure
- Sialic acid
- α 2-6-Sialyltransferase
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology
Cite this
Crystal structures of sialyltransferase from Photobacterium damselae. / Huynh, Nhung; Li, Yanhong; Yu, Hai; Huang, Shengshu; Lau, Kam; Chen, Xi; Fisher, Andrew J.
In: FEBS Letters, Vol. 588, No. 24, 20.12.2014, p. 4720-4729.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystal structures of sialyltransferase from Photobacterium damselae
AU - Huynh, Nhung
AU - Li, Yanhong
AU - Yu, Hai
AU - Huang, Shengshu
AU - Lau, Kam
AU - Chen, Xi
AU - Fisher, Andrew J
PY - 2014/12/20
Y1 - 2014/12/20
N2 - 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.
AB - 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.
KW - CMP-3F(a)Neu5Ac
KW - Photobacterium damselae
KW - Protein crystal structure
KW - Sialic acid
KW - α 2-6-Sialyltransferase
UR - http://www.scopus.com/inward/record.url?scp=84915745108&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84915745108&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2014.11.003
DO - 10.1016/j.febslet.2014.11.003
M3 - Article
C2 - 25451227
AN - SCOPUS:84915745108
VL - 588
SP - 4720
EP - 4729
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 24
ER -