1EHI

D-ALANINE:D-LACTATE LIGASE (LMDDL2) OF VANCOMYCIN-RESISTANT LEUCONOSTOC MESENTEROIDES

Summary for 1EHI

• Entry DOI: 10.2210/pdb1ehi/pdb
• Related: 1IOV 1IOW 2DLN
• Descriptor: D-ALANINE:D-LACTATE LIGASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: atp-binding. grasp motif for atp., ligase
• Biological source: Leuconostoc mesenteroides
• Cellular location: Cytoplasm : P71454
• Total number of polymer chains: 2
• Total formula weight: 84484.71

Authors

Kuzin, A.P.,Sun, T.,Jorczak-Baillass, J.,Healy, V.L.,Walsh, C.T.,Knox, J.R. (deposition date: 2000-02-21, release date: 2000-05-23, Last modification date: 2024-03-13)

Primary citation

Kuzin, A.P.,Sun, T.,Jorczak-Baillass, J.,Healy, V.L.,Walsh, C.T.,Knox, J.R.
Enzymes of vancomycin resistance: the structure of D-alanine-D-lactate ligase of naturally resistant Leuconostoc mesenteroides.
Structure Fold.Des., 8:463-470, 2000

PubMed Abstract: The bacterial cell wall and the enzymes that synthesize it are targets of glycopeptide antibiotics (vancomycins and teicoplanins) and beta-lactams (penicillins and cephalosporins). Biosynthesis of cell wall peptidoglycan requires a crosslinking of peptidyl moieties on adjacent glycan strands. The D-alanine-D-alanine transpeptidase, which catalyzes this crosslinking, is the target of beta-lactam antibiotics. Glycopeptides, in contrast, do not inhibit an enzyme, but bind directly to D-alanine-D-alanine and prevent subsequent crosslinking by the transpeptidase. Clinical resistance to vancomycin in enterococcal pathogens has been traced to altered ligases producing D-alanine-D-lactate rather than D-alanine-D-alanine.

PubMed: 10801495
DOI: 10.1016/S0969-2126(00)00129-5

Experimental method

X-RAY DIFFRACTION (2.38 Å)