PDBsum entry 4m9c

Transferase

PDB id: 4m9c

Contents

Protein chains

(+ 0 more) 216 a.a.

Waters ×640

PDB id:

4m9c

Name:

Transferase

Title:

Weei from acinetobacter baumannii aye

Structure:

Bacterial transferase hexapeptide (three repeats) family protein. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Acinetobacter baumannii. Organism_taxid: 470. Strain: aye. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.10Å R-factor: 0.193 R-free: 0.226

Authors:

M.J.Morrison,B.Imperiali

Key ref:

M.J.Morrison and B.Imperiali (2013). Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine. J Biol Chem, 288, 32248-32260. PubMed id: 24064219 DOI: 10.1074/jbc.M113.510560

Date:

14-Aug-13 Release date: 02-Oct-13

Protein chains

B0V6J7  (B0V6J7_ACIBY) -  Acetyltransferase (WeeI) from Acinetobacter baumannii (strain AYE)

Seq: 216 a.a.

Struc: 216 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.1.- - ?????

DOI no: 10.1074/jbc.M113.510560

J Biol Chem 288:32248-32260 (2013)

PubMed id: 24064219

Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine.

M.J.Morrison, B.Imperiali.

ABSTRACT

UDP-N,N'-diacetylbacillosamine (UDP-diNAcBac) is a unique carbohydrate produced by a number of bacterial species and has been implicated in pathogenesis. The terminal step in the formation of this important bacterial sugar is catalyzed by an acetyl-CoA (AcCoA)-dependent acetyltransferase in both N- and O-linked protein glycosylation pathways. This bacterial acetyltransferase is a member of the left-handed β-helix family and forms a homotrimer as the functional unit. Whereas previous endeavors have focused on the Campylobacter jejuni acetyltransferase (PglD) from the N-linked glycosylation pathway, structural characterization of the homologous enzymes in the O-linked glycosylation pathways is lacking. Herein, we present the apo-crystal structures of the acetyltransferase domain (ATD) from the bifunctional enzyme PglB (Neisseria gonorrhoeae) and the full-length acetyltransferase WeeI (Acinetobacter baumannii). Additionally, a PglB-ATD structure was solved in complex with AcCoA. Surprisingly, this structure reveals a contrasting binding mechanism for this substrate when compared with the AcCoA-bound PglD structure. A comparison between these findings and the previously solved PglD crystal structures illustrates a dichotomy among N- and O-linked glycosylation pathway enzymes. Based upon these structures, key residues in the UDP-4-amino and AcCoA binding pockets were mutated to determine their effect on binding and catalysis in PglD, PglB-ATD, and WeeI. Last, a phylogenetic analysis of the aforementioned acetyltransferases was employed to illuminate the diversity among N- and O-linked glycosylation pathway enzymes.