|
type |
Journal Article |
authors |
Riegert AS, Young NM, Watson DC, Thoden JB, Holden HM |
title |
Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis |
journal |
Protein Sci |
Activity |
2.6.1.34 |
Family |
2.6.1.34.a |
sel |
selected |
ui |
26178292 |
year |
(2015) |
volume |
24 |
number |
10 |
pages |
1609-16 |
| |
keywords |
N,N'-diacetylbacillosamine; N-glycosylation; aminotransferase; bacterial glycoproteins; pyridoxal 5'-phosphate |
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. |
last changed |
2019/12/04 09:59 |
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