1GHE

CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A

Summary for 1GHE

• Entry DOI: 10.2210/pdb1ghe/pdb
• Descriptor: ACETYLTRANSFERASE, ACETYL COENZYME *A (3 entities in total)
• Functional Keywords: acyl coenzyme a complex, transferase
• Biological source: Pseudomonas syringae pv. tabaci
• Total number of polymer chains: 2
• Total formula weight: 40604.03

Authors

He, H.,Ding, Y.,Bartlam, M.,Sun, F.,Le, Y.,Qin, X.,Tang, H.,Zhang, R.,Joachimiak, A.,Liu, Y.,Zhao, N.,Rao, Z. (deposition date: 2000-12-13, release date: 2003-01-14, Last modification date: 2024-11-06)

Primary citation

He, H.,Ding, Y.,Bartlam, M.,Sun, F.,Le, Y.,Qin, X.,Tang, H.,Zhang, R.,Joachimiak, A.,Liu, Y.,Zhao, N.,Rao, Z.
Crystal Structure of Tabtoxin Resistance Protein Complexed with Acetyl Coenzyme A Reveals the Mechanism for beta-Lactam Acetylation
J.Mol.Biol., 325:1019-1030, 2003

PubMed Abstract: Tabtoxin resistance protein (TTR) is an enzyme that renders tabtoxin-producing pathogens, such as Pseudomonas syringae, tolerant to their own phytotoxins. Here, we report the crystal structure of TTR complexed with its natural cofactor, acetyl coenzyme A (AcCoA), to 1.55A resolution. The binary complex forms a characteristic "V" shape for substrate binding and contains the four motifs conserved in the GCN5-related N-acetyltransferase (GNAT) superfamily, which also includes the histone acetyltransferases (HATs). A single-step mechanism is proposed to explain the function of three conserved residues, Glu92, Asp130 and Tyr141, in catalyzing the acetyl group transfer to its substrate. We also report that TTR possesses HAT activity and suggest an evolutionary relationship between TTR and other GNAT members.

PubMed: 12527305
DOI: 10.1016/S0022-2836(02)01284-6

Experimental method

X-RAY DIFFRACTION (1.55 Å)