2G2O

Structure of E.coli FabD complexed with sulfate

Summary for 2G2O

• Entry DOI: 10.2210/pdb2g2o/pdb
• Related: 2G2Y
• Descriptor: Malonyl CoA-acyl carrier protein transacylase, SULFATE ION (3 entities in total)
• Functional Keywords: complex, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 32407.94

Authors

Oefner, C. (deposition date: 2006-02-16, release date: 2006-05-30, Last modification date: 2024-03-13)

Primary citation

Oefner, C.,Schulz, H.,D'Arcy, A.,Dale, G.E.
Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography.
Acta Crystallogr.,Sect.D, 62:613-618, 2006

PubMed Abstract: Malonyl-CoA-acyl carrier protein transacylase (FabD; EC 2.3.1.39) is a key enzyme in the fatty-acid biosynthesis pathway of bacteria, catalyzing the transfer of a malonyl moiety from malonyl-CoA to holo acyl carrier protein (ACP), generating malonyl-ACP and free CoASH. Malonyl-ACP, which is the product of this reaction, is the key building block for de novo fatty-acid biosynthesis. Various binary complex structures of the Escherichia coli enzyme are presented, including that of the natural substrate malonyl-CoA, indicating the functional role of the highly conserved amino acids Gln11, Ser92, Arg117 and His201 and the stabilizing function of the preformed oxyanion hole during the enzymatic reaction. Based on the presented structural data, a possible new catalytic enzyme mechanism is discussed. The data obtained could be used in aiding the process of rational inhibitor design.

PubMed: 16699188
DOI: 10.1107/S0907444906009474

Experimental method

X-RAY DIFFRACTION (1.76 Å)