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Title: Crystal structures of sialyltransferase from Photobacterium damselae

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. In this paper, 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. Finally, comparison of the three structures reveals small inherent flexibility between the two Rossmann-like domains of the GT-B fold.
Authors:
 [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [1]
  1. Univ. of California, Davis, CA (United States)
Publication Date:
OSTI Identifier:
1347143
Grant/Contract Number:
R01HD065122; R01GM094523; P41GM103393; P41RR001209
Type:
Accepted Manuscript
Journal Name:
FEBS Letters
Additional Journal Information:
Journal Volume: 588; Journal Issue: 24; Journal ID: ISSN 0014-5793
Publisher:
Federation of European Biochemical Societies
Research Org:
Univ. of California, Davis, CA (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Inst. of Health (NIH) (United States)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; α2–6-sialyltransferase; protein crystal structure; sialic acid; CMP-3F(a)Neu5Ac; Photobacterium damselae