PDBsum entry 4ztc

Transferase

PDB id: 4ztc

Contents

Protein chain

385 a.a.

Ligands

4RA

Waters ×275

PDB id:

4ztc

Name:

Transferase

Title:

Pgle aminotransferase in complex with external aldimine, mutant k184a

Structure:

Aminotransferase homolog. Chain: a. Engineered: yes. Mutation: yes

Source:

Campylobacter jejuni. Organism_taxid: 197. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.192 R-free: 0.254

Authors:

A.S.Riegert,J.B.Thoden,N.M.Young,D.C.Watson,H.M.Holden

Key ref:

A.S.Riegert et al. (2015). Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis. Protein Sci, 24, 1609-1616. PubMed id: 26178292 DOI: 10.1002/pro.2745

Date:

14-May-15 Release date: 29-Jul-15

Protein chain

Q0P9D3  (PGLE_CAMJE) -  UDP-N-acetylbacillosamine transaminase from Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

Seq: 386 a.a.

Struc: 385 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.6.1.34 - UDP-N-acetylbacillosamine transaminase.
• Reaction: UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy- alpha-D-xylo-hex-4-ulose + L-glutamate
• Cofactor: Pyridoxal 5'-phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1002/pro.2745

Protein Sci 24:1609-1616 (2015)

PubMed id: 26178292

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

A.S.Riegert, N.M.Young, D.C.Watson, J.B.Thoden, H.M.Holden.

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.