Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1

Anna M Davies; Renée Tata; Alison Snape; Brian J Sutton; Paul R Brown

doi:10.1016/j.biochi.2008.12.003

Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1

Biochimie. 2009 Apr;91(4):484-9. doi: 10.1016/j.biochi.2008.12.003. Epub 2008 Dec 24.

Authors

Anna M Davies¹, Renée Tata, Alison Snape, Brian J Sutton, Paul R Brown

Affiliation

¹ King's College London, Randall Division of Cell and Molecular Biophysics, London, SE1 1UL, UK.

PMID: 19135125
DOI: 10.1016/j.biochi.2008.12.003

Abstract

Gene ACIAD1637 from Acinetobacter baylyi ADP1 encodes a 182 amino acid putative antibiotic resistance protein. The structure of this protein (termed acepita) has been solved in space group P(2) to 2.35 A resolution. Acepita belongs to the GCN5-related N-acetyltransferase (GNAT) family, and contains the four sequence motifs conserved among family members. The structure of acepita is compared with that of pita, its homologue from Pseudomonas aeruginosa. Acepita has a similar substrate profile to pita and performs a similar function.

MeSH terms

Acetyltransferases / chemistry*
Acetyltransferases / genetics
Acetyltransferases / metabolism*
Acinetobacter / enzymology*
Acinetobacter / metabolism
Amino Acid Sequence
Catalytic Domain / physiology*
Crystallization
Kinetics
Molecular Sequence Data
Molecular Structure
Mutation / genetics
Sequence Alignment
Substrate Specificity / physiology

Substances

Acetyltransferases