4uag
From Proteopedia
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- | [[Image:4uag.jpg|left|200px]] | + | [[Image:4uag.jpg|left|200px]] |
- | + | ||
- | '''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE''' | + | {{Structure |
+ | |PDB= 4uag |SIZE=350|CAPTION= <scene name='initialview01'>4uag</scene>, resolution 1.660Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UAG:URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE-D-GLUTAMATE'>UAG</scene> and <scene name='pdbligand=UNX:UNKNOWN ATOM OR ION'>UNX</scene> | ||
+ | |ACTIVITY= [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] | ||
+ | |GENE= MURD GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | }} | ||
+ | |||
+ | '''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 4UAG is a [ | + | 4UAG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UAG OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10356330 10356330] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:11:15 2008'' |
Revision as of 17:11, 20 March 2008
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, resolution 1.660Å | |||||||
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Ligands: | , and | ||||||
Gene: | MURD GENE (Escherichia coli) | ||||||
Activity: | UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase, with EC number 6.3.2.9 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
Overview
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.
About this Structure
4UAG 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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