Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis

DOI	Resolve DOI: https://doi.org/10.1002/pro.2745
Author	Search for: Riegert, Alexander S.; Search for: Young, N. Martin¹; Search for: Watson, David C.¹; Search for: Thoden, James B.; Search for: Holden, Hazel M.
Name affiliation	National Research Council Canada. Human Health Therapeutics
Format	Text
Type	Article
Journal title	Protein Science
ISSN	0961-8368
Volume	24
Issue	10
Pages	1609–1616; # of pages: 8
Abstract	N,N'-diacetylbacillosamine is a novel sugar that plays a key role in bacterial glycosylation. Three enzymes are required for its biosynthesis in Campylobacter jejuni starting from UDP-GlcNAc. The focus of this investigation, PglE, catalyzes the second step in the pathway. It is a PLP-dependent aminotransferase that converts UDP-2-acetamido-4-keto-2,4,6-trideoxy-d-glucose to UDP-2-acetamido-4-amino-2,4,6-trideoxy-d-glucose. For this investigation, the structure of PglE in complex with an external aldimine was determined to a nominal resolution of 2.0 Å. A comparison of its structure with those of other sugar aminotransferases reveals a remarkable difference in the manner by which PglE accommodates its nucleotide-linked sugar substrate.
Publication date	2015-07-14
Publisher	Wiley
Language	English
Peer reviewed	Yes
NPARC number	21277361
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Record identifier	b84455c9-b8a9-4eb6-8f0e-b9b8286586bc
Record created	2016-03-09
Record modified	2016-05-09