Crystallization (Comment) | Organism |
---|---|
PseH alone and in complex with AcCoA, to 1.95 A resolution. PseH folds into a single-domain structure of a central beta-sheet decorated by four alpha-helices with two continuously connected grooves. A deep groove accommodates the AcCoA molecule. The acetyl end of AcCoA points toward an open space in a neighboring shallow groove, which is occupied by extra electron density that potentially serves as a pseudosubstrate. PseH may utilize a catalytic mechanism of acetylation different from other glycosylation-associated acetyltransferases | Campylobacter jejuni |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | A0A0J9X276 | subsp. jejuni | - |
Campylobacter jejuni PT14 | A0A0J9X276 | subsp. jejuni | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine | - |
Campylobacter jejuni | CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose | - |
? | |
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine | - |
Campylobacter jejuni PT14 | CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose | - |
? |
Synonyms | Comment | Organism |
---|---|---|
A911_06385 | - |
Campylobacter jejuni |