 |
PDBsum entry 4ztc
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structure of the external aldimine form of pgle, An aminotransferase required for n,N'-Diacetylbacillosamine biosynthesis.
|
 |
|
Authors
|
 |
A.S.Riegert,
N.M.Young,
D.C.Watson,
J.B.Thoden,
H.M.Holden.
|
 |
|
Ref.
|
 |
Protein Sci, 2015,
24,
1609-1616.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
|
|
|
 |