2ft0
From Proteopedia
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'''Crystal structure of TDP-fucosamine acetyltransferase (WecD)- complex with acetyl-CoA''' | '''Crystal structure of TDP-fucosamine acetyltransferase (WecD)- complex with acetyl-CoA''' | ||
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[[Category: Rangarajan, E.]] | [[Category: Rangarajan, E.]] | ||
[[Category: Sulea, T.]] | [[Category: Sulea, T.]] | ||
| - | [[Category: | + | [[Category: Bsgi]] |
| - | [[Category: | + | [[Category: Gnat fold acetyltransferase]] |
| - | [[Category: | + | [[Category: Montreal-kingston bacterial structural genomics initiative]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:16:56 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:16, 4 May 2008
Crystal structure of TDP-fucosamine acetyltransferase (WecD)- complex with acetyl-CoA
Overview
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.
About this Structure
2FT0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis., Hung MN, Rangarajan E, Munger C, Nadeau G, Sulea T, Matte A, J Bacteriol. 2006 Aug;188(15):5606-17. PMID:16855251 Page seeded by OCA on Sun May 4 04:16:56 2008
Categories: Escherichia coli | Single protein | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Hung, M N. | Matte, A. | Munger, C. | Nadeau, G. | Rangarajan, E. | Sulea, T. | Bsgi | Gnat fold acetyltransferase | Montreal-kingston bacterial structural genomics initiative | Structural genomic
