2uag

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{{STRUCTURE_2uag| PDB=2uag | SCENE= }}
{{STRUCTURE_2uag| PDB=2uag | SCENE= }}
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'''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE'''
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===UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10356330}}
==About this Structure==
==About this Structure==
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[[Category: Murd]]
[[Category: Murd]]
[[Category: Peptidoglycan synthesis]]
[[Category: Peptidoglycan synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:46:20 2008''

Revision as of 06:46, 29 July 2008

Image:2uag.png

Template:STRUCTURE 2uag

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

Template:ABSTRACT PUBMED 10356330

About this Structure

2UAG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Determination of the MurD mechanism through crystallographic analysis of enzyme complexes., Bertrand JA, Auger G, Martin L, Fanchon E, Blanot D, Le Beller D, van Heijenoort J, Dideberg O, J Mol Biol. 1999 Jun 11;289(3):579-90. PMID:10356330

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