1eeh
From Proteopedia
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UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
Overview
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.
About this Structure
1EEH is a Single protein structure of sequence from Escherichia coli with UMA as ligand. Active as UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase, with EC number 6.3.2.9 Full crystallographic information is available from OCA.
Reference
"Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase., Bertrand JA, Fanchon E, Martin L, Chantalat L, Auger G, Blanot D, van Heijenoort J, Dideberg O, J Mol Biol. 2000 Sep 1;301(5):1257-66. PMID:10966819
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