2ft0: Difference between revisions

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[[Image:2ft0.gif|left|200px]]
{{Seed}}
[[Image:2ft0.png|left|200px]]


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{{STRUCTURE_2ft0|  PDB=2ft0  |  SCENE=  }}  
{{STRUCTURE_2ft0|  PDB=2ft0  |  SCENE=  }}  


'''Crystal structure of TDP-fucosamine acetyltransferase (WecD)- complex with acetyl-CoA'''
===Crystal structure of TDP-fucosamine acetyltransferase (WecD)- complex with acetyl-CoA===




==Overview==
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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 --&gt;3)-alpha-d-Fuc4NAc-(1--&gt;4)-beta-d-ManNAcA-(1--&gt;4)-alpha-d-GlcNAc-(1--&gt;. 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.
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{{ABSTRACT_PUBMED_16855251}}


==About this Structure==
==About this Structure==
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[[Category: Montreal-kingston bacterial structural genomics initiative]]
[[Category: Montreal-kingston bacterial structural genomics initiative]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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