4ztc
PglE Aminotransferase in complex with External Aldimine, Mutant K184A
Structural highlights
FunctionPGLE_CAMJE Aminotransferase involved in the bacillosamine biosynthesis pathway by producing UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc (UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose), a precursor used in the production of the glycan component 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose. Required for host colonization and virulence. Involved in the N-linked protein glycosylation pathway.[1] [2] Publication Abstract from PubMedN,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. 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. This article is protected by copyright. All rights reserved. Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.,Riegert AS, Young NM, Watson DC, Thoden JB, Holden HM Protein Sci. 2015 Jul 14. doi: 10.1002/pro.2745. PMID:26178292[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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