2jfg: Difference between revisions

Mur ligases play an essential role in the intracellular biosynthesis of, bacterial peptidoglycan, the main component of the bacterial cell wall, and represent attractive targets for the design of novel antibacterials., UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) catalyses the, addition of D-glutamic acid to the cytoplasmic intermediate, UDP-N-acetylmuramoyl-L-alanine (UMA) and is the second in the series of, Mur ligases. MurD ligase is highly stereospecific for its substrate, D-glutamic acid (D-Glu). Here, we report the high resolution crystal, structures of MurD in complexes with two novel inhibitors designed to, mimic the transition state of the reaction, which contain either the D-Glu, or the L-Glu moiety. The binding modes of N-sulfonyl-D-Glu and, N-sulfonyl-L-Glu derivatives were also characterised kinetically. The, results of this study represent an excellent starting point for further, development of novel inhibitors of this enzyme.

2JFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4, UMA and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanine--D-glutamate_ligase UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.9 6.3.2.9] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JFG OCA].  

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