Crystal structure of bacillus subtilis YdaF protein : a putative ribosomal N-acetyltransferase.
Comparative sequence analysis suggests that the ydaF gene encodes a protein (YdaF) that functions as an N-acetyltransferase, more specifically, a ribosomal N-acetyltransferase. Sequence analysis using basic local alignment search tool (BLAST) suggests that YdaF belongs to a large family of proteins (199 proteins found in 88 unique species of bacteria, archaea, and eukaryotes). YdaF also belongs to the COG1670, which includes the Escherichia coli RimL protein that is known to acetylate ribosomal protein L12. N-acetylation (NAT) has been found in all kingdoms. NAT enzymes catalyze the transfer of an acetyl group from acetyl-CoA (AcCoA) to a primary amino group. For example, NATs can acetylate the N-terminal {alpha}-amino group, the {epsilon}-amino group of lysine residues, aminoglycoside antibiotics, spermine/speridine, or arylalkylamines such as serotonin. The crystal structure of the alleged ribosomal NAT protein, YdaF, from Bacillus subtilis presented here was determined as a part of the Midwest Center for Structural Genomics. The structure maintains the conserved tertiary structure of other known NATs and a high sequence similarity in the presumed AcCoA binding pocket in spite of a very low overall level of sequence identity to other NATs of known structure.
- Research Organization:
- Argonne National Laboratory (ANL)
- Sponsoring Organization:
- SC; NIH
- DOE Contract Number:
- AC02-06CH11357
- OSTI ID:
- 961398
- Report Number(s):
- ANL/BIO/JA-47423
- Journal Information:
- Proteins: Struct. Function Bioinform., Journal Name: Proteins: Struct. Function Bioinform. Journal Issue: 4 ; Dec. 1, 2004 Vol. 57
- Country of Publication:
- United States
- Language:
- ENGLISH
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