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Structure of the external aldimine form of PglE, an aminotransferase required for N , N '‐diacetylbacillosamine biosynthesis
Author(s) -
Riegert Alexander S.,
Young N. Martin,
Watson David C.,
Thoden James B.,
Holden Hazel M.
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2745
Subject(s) - aldimine , biosynthesis , stereochemistry , chemistry , enzyme , biochemistry , catalysis
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.