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B6db references: 26178292

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 . 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

B6db references