4ZTC

Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.

(2015) Protein Sci 24: 1609-1616

• PubMed: 26178292 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1002/pro.2745
• Primary Citation of Related Structures:  
  4ZTC


• PubMed 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.

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Organizational Affiliation: 

Department of Biochemistry, University of Wisconsin, Madison, Wisconsin, 53706.