1eeh

<table><tr><td colspan='2'>[[1eeh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EEH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UMA:URIDINE-5-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE'>UMA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uag|1uag]], [[2uag|2uag]], [[3uag|3uag]], [[4uag|4uag]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanine--D-glutamate_ligase UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.9 6.3.2.9] </span></td></tr>

[[https://www.uniprot.org/uniprot/MURD_ECOLI MURD_ECOLI]] Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).[HAMAP-Rule:MF_00639]

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== Publication Abstract from PubMed ==

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.

"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<ref>PMID:10966819</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1eeh" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Auger, G]]

[[Category: Bertrand, J A]]

[[Category: Blanot, D]]

[[Category: Chantalat, L]]

[[Category: Dideberg, O]]

[[Category: Fanchon, E]]

[[Category: Heijenoort, J van]]

[[Category: Martin, L]]

[[Category: Adp-forming enzyme]]

[[Category: Peptidoglycan synthesis]]