1EEH

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

Summary for 1EEH

• Entry DOI: 10.2210/pdb1eeh/pdb
• Related: 1UAG 2UAG 3UAG 4UAG
• Descriptor: UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE (3 entities in total)
• Functional Keywords: ligase, peptidoglycan synthesis, murd, adp-forming enzyme
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P14900
• Total number of polymer chains: 1
• Total formula weight: 47639.74

Authors

Bertrand, J.A.,Fanchon, E.,Martin, L.,Chantalat, L.,Auger, G.,Blanot, D.,van Heijenoort, J.,Dideberg, O. (deposition date: 2000-01-31, release date: 2001-01-17, Last modification date: 2024-02-07)

Primary citation

Bertrand, J.A.,Fanchon, E.,Martin, L.,Chantalat, L.,Auger, G.,Blanot, D.,van Heijenoort, J.,Dideberg, O.
"Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase.
J.Mol.Biol., 301:1257-1266, 2000

PubMed Abstract: UDP-N-acetylmuramoyl-l-alanine:d-glutamate (MurD) ligase catalyses the addition of d-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-l-alanine (UMA). The crystal structures of Escherichia coli in the substrate-free form and MurD complexed with UMA have been determined at 2.4 A and 1.88 A resolution, respectively. The MurD structure comprises three domains each of a topology reminiscent of nucleotide-binding folds. In the two structures the C-terminal domain undergoes a large rigid-body rotation away from the N-terminal and central domains. These two "open" structures were compared with the four published "closed" structures of MurD. In addition the comparison reveals which regions are affected by the binding of UMA, ATP and d-Glu. Also we compare and discuss two structurally characterized enzymes which belong to the same ligase superfamily: MurD and folylpolyglutamate synthetase (FGS). The analysis allows the identification of key residues involved in the reaction mechanism of FGS. The determination of the two "open" conformation structures represents a new step towards the complete elucidation of the enzymatic mechanism of the MurD ligase.

PubMed: 10966819
DOI: 10.1006/jmbi.2000.3994

Experimental method

X-RAY DIFFRACTION (1.9 Å)