2FS5

Crystal structure of TDP-fucosamine acetyltransferase (WecD)- apo form

Summary for 2FS5

• Entry DOI: 10.2210/pdb2fs5/pdb
• Related: 2ft0
• Descriptor: TDP-Fucosamine acetyltransferase, ZINC ION (3 entities in total)
• Functional Keywords: gnat fold, acetyltransferase, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 50952.44

Authors

Hung, M.N.,Rangarajan, E.,Munger, C.,Nadeau, G.,Sulea, T.,Matte, A.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2006-01-20, release date: 2006-08-01, Last modification date: 2024-02-14)

Primary citation

Hung, M.N.,Rangarajan, E.,Munger, C.,Nadeau, G.,Sulea, T.,Matte, A.
Crystal Structure of TDP-Fucosamine Acetyltransferase (WecD) from Escherichia coli, an Enzyme Required for Enterobacterial Common Antigen Synthesis.
J.Bacteriol., 188:5606-5617, 2006

PubMed Abstract: Enterobacterial common antigen (ECA) is a polysaccharide found on the outer membrane of virtually all gram-negative enteric bacteria and consists of three sugars, N-acetyl-d-glucosamine, N-acetyl-d-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-d-galactose, organized into trisaccharide repeating units having the sequence -->3)-alpha-d-Fuc4NAc-(1-->4)-beta-d-ManNAcA-(1-->4)-alpha-d-GlcNAc-(1-->. While the precise function of ECA is unknown, it has been linked to the resistance of Shiga-toxin-producing Escherichia coli (STEC) O157:H7 to organic acids and the resistance of Salmonella enterica to bile salts. The final step in the synthesis of 4-acetamido-4,6-dideoxy-d-galactose, the acetyl-coenzyme A (CoA)-dependent acetylation of the 4-amino group, is carried out by TDP-fucosamine acetyltransferase (WecD). We have determined the crystal structure of WecD in apo form at a 1.95-Angstrom resolution and bound to acetyl-CoA at a 1.66-Angstrom resolution. WecD is a dimeric enzyme, with each monomer adopting the GNAT N-acetyltransferase fold, common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars. The crystal structure of WecD, however, represents the first structure of a GNAT family member that acts on nucleotide sugars. Based on this cocrystal structure, we have used flexible docking to generate a WecD-bound model of the acetyl-CoA-TDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. Our structural data show that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of coenzyme A.

PubMed: 16855251
DOI: 10.1128/JB.00306-06

Experimental method

X-RAY DIFFRACTION (1.95 Å)