Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4IK0

Crystal structure of diaminopimelate epimerase Y268A mutant from Escherichia coli

Summary for 4IK0
Entry DOI10.2210/pdb4ik0/pdb
Related4IJZ
DescriptorDiaminopimelate epimerase, IODIDE ION (3 entities in total)
Functional Keywordsdap epimerase-like, isomerase, cytosol
Biological sourceEscherichia coli
Cellular locationCytoplasm: P0A6K1
Total number of polymer chains2
Total formula weight63614.40
Authors
Hor, L.,Dobson, R.C.J.,Hutton, C.A.,Perugini, M.A. (deposition date: 2012-12-24, release date: 2013-02-20, Last modification date: 2024-03-20)
Primary citationHor, L.,Dobson, R.C.J.,Downton, M.T.,Wagner, J.,Hutton, C.A.,Perugini, M.A.
Dimerization of bacterial diaminopimelate epimerase is essential for catalysis
J.Biol.Chem., 288:9238-9248, 2013
Cited by
PubMed Abstract: Diaminopimelate (DAP) epimerase is involved in the biosynthesis of meso-DAP and lysine, which are important precursors for the synthesis of peptidoglycan, housekeeping proteins, and virulence factors in bacteria. Accordingly, DAP epimerase is a promising antimicrobial target. Previous studies report that DAP epimerase exists as a monomeric enzyme. However, we show using analytical ultracentrifugation, X-ray crystallography, and enzyme kinetic analyses that DAP epimerase from Escherichia coli exists as a functional dimer in solution and the crystal state. Furthermore, the 2.0-Å X-ray crystal structure of the E. coli DAP epimerase dimer shows for the first time that the enzyme exists in an open, active conformation. The importance of dimerization was subsequently probed by using site-directed mutagenesis to generate a monomeric mutant (Y268A). Our studies show that Y268A is catalytically inactive, thus demonstrating that dimerization of DAP epimerase is essential for catalysis. Molecular dynamics simulations indicate that the DAP epimerase monomer is inherently more flexible than the dimer, suggesting that dimerization optimizes protein dynamics to support function. Our findings offer insight into the development of novel antimicrobial agents targeting the dimeric antibiotic target DAP epimerase.
PubMed: 23426375
DOI: 10.1074/jbc.M113.450148
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon