2JLM

Structure of a Putative Acetyltransferase (ACIAD1637) from Acinetobacter baylyi ADP1

Summary for 2JLM

• Entry DOI: 10.2210/pdb2jlm/pdb
• Descriptor: PUTATIVE PHOSPHINOTHRICIN N-ACETYLTRANSFERASE, ACETATE ION, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• Functional Keywords: phosphinothricin, acetyltransferase, transferase, methionine sulfoximine
• Biological source: ACINETOBACTER BAYLYI
• Total number of polymer chains: 6
• Total formula weight: 125621.21

Authors

Davies, A.M.,Tata, R.,Snape, A.,Sutton, B.J.,Brown, P.R. (deposition date: 2008-09-10, release date: 2009-01-20, Last modification date: 2023-12-13)

Primary citation

Davies, A.M.,Tata, R.,Snape, A.,Sutton, B.J.,Brown, P.R.
Structure and Substrate Specificity of Acetyltransferase Aciad1637 from Acinetobacter Baylyi Adp1.
Biochimie, 91:484-, 2009

PubMed 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.

PubMed: 19135125
DOI: 10.1016/J.BIOCHI.2008.12.003

Experimental method

X-RAY DIFFRACTION (2.35 Å)