Determination of the MurD mechanism through crystallographic analysis of enzyme complexes. Export

@article{Bertrand99, 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 three complexes of Escherichia coli MurD with a variety of substrates and products have been determined to high resolution. These include (1) the quaternary complex of MurD, the substrate UMA, the product ADP, and Mg2+, (2) the quaternary complex of MurD, the substrate UMA, the product ADP, and Mn2+, and (3) the binary complex of MurD with the product UDP - N- acetylmuramoyl- L -alanine- D -glutamate (UMAG). The reaction mechanism supported by these structures proceeds by the phosphorylation of the C-terminal carboxylate group of UMA by the gamma-phosphate group of ATP to form an acyl-phosphate intermediate, followed by the nucleophilic attack by the amino group of D-glutamate to produce UMAG. A key feature in the reaction intermediate is the presence of two magnesium ions bridging negatively charged groups.}, author = {Bertrand, J. A. and Auger, G. and Martin, L. and Fanchon, E. and Blanot, D. and Le Beller, D. and van Heijenoort, J. and Dideberg, O.}, citeulike-article-id = {388938}, journal = {J Mol Biol}, keywords = {crystal\_structure, enzyme, ligase, mechanism}, number = {3}, pages = {579--90}, posted-at = {2005-11-11 16:23:16}, priority = {2}, title = {Determination of the {M}ur{D} mechanism through crystallographic analysis of enzyme complexes.}, volume = {289}, year = {1999} }

TY - JOUR ID - Bertrand99 L3 - citeulike-article-id:388938 N2 - 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 three complexes of Escherichia coli MurD with a variety of substrates and products have been determined to high resolution. These include (1) the quaternary complex of MurD, the substrate UMA, the product ADP, and Mg2+, (2) the quaternary complex of MurD, the substrate UMA, the product ADP, and Mn2+, and (3) the binary complex of MurD with the product UDP - N- acetylmuramoyl- L -alanine- D -glutamate (UMAG). The reaction mechanism supported by these structures proceeds by the phosphorylation of the C-terminal carboxylate group of UMA by the gamma-phosphate group of ATP to form an acyl-phosphate intermediate, followed by the nucleophilic attack by the amino group of D-glutamate to produce UMAG. A key feature in the reaction intermediate is the presence of two magnesium ions bridging negatively charged groups. IS - 3 JF - J Mol Biol EP - 90 TI - Determination of the {M}ur{D} mechanism through crystallographic analysis of enzyme complexes. VL - 289 SP - 579 KW - crystal_structure KW - enzyme KW - ligase KW - mechanism AU - Bertrand, JA AU - Auger, G AU - Martin, L AU - Fanchon, E AU - Blanot, D AU - Le Beller, D AU - van Heijenoort, J AU - Dideberg, O PY - 1999/// ER -