4ZTC

PglE Aminotransferase in complex with External Aldimine, Mutant K184A

Summary for 4ZTC

• Entry DOI: 10.2210/pdb4ztc/pdb
• Descriptor: Aminotransferase homolog, [(2R,3R,4R,5S,6R)-3-acetamido-6-methyl-5-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-4-oxidanyl-oxan-2-yl] [[(2R,3S,4R,5R)-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] hydrogen phosphate (3 entities in total)
• Functional Keywords: aminotransferase, n-n'-diacetylbacillosamine, n-glycosylation pyridoxyl 5'-phosphate, transferase
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 1
• Total formula weight: 44618.70

Authors

Riegert, A.S.,Thoden, J.B.,Young, N.M.,Watson, D.C.,Holden, H.M. (deposition date: 2015-05-14, release date: 2015-07-29, Last modification date: 2023-09-27)

Primary citation

Riegert, A.S.,Young, N.M.,Watson, D.C.,Thoden, J.B.,Holden, H.M.
Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.
Protein Sci., 24:1609-1616, 2015

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 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.

PubMed: 26178292
DOI: 10.1002/pro.2745

Experimental method

X-RAY DIFFRACTION (2 Å)