1eeh

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{{STRUCTURE_1eeh| PDB=1eeh | SCENE= }}
{{STRUCTURE_1eeh| PDB=1eeh | 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 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.
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{{ABSTRACT_PUBMED_10966819}}
==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 1 00:34:14 2008''

Revision as of 21:34, 30 June 2008

Image:1eeh.png

Template:STRUCTURE 1eeh

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

Template:ABSTRACT PUBMED 10966819

About this Structure

1EEH is a Single protein structure of sequence from Escherichia coli. 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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