4uag
From Proteopedia
(New page: 200px<br /><applet load="4uag" size="450" color="white" frame="true" align="right" spinBox="true" caption="4uag, resolution 1.660Å" /> '''UDP-N-ACETYLMURAMOY...) |
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| - | [[Image:4uag.jpg|left|200px]]<br /><applet load="4uag" size=" | + | [[Image:4uag.jpg|left|200px]]<br /><applet load="4uag" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="4uag, resolution 1.660Å" /> | caption="4uag, resolution 1.660Å" /> | ||
'''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE'''<br /> | '''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | UDP -N- acetylmuramoyl- L -alanine: D -glutamate (MurD) ligase catalyses | + | 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== | ==About this Structure== | ||
| - | 4UAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4, UAG and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 4UAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=UAG:'>UAG</scene> and <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UAG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase]] | [[Category: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase]] | ||
[[Category: Auger, G.]] | [[Category: Auger, G.]] | ||
| - | [[Category: Beller, D | + | [[Category: Beller, D Le.]] |
[[Category: Bertrand, J.]] | [[Category: Bertrand, J.]] | ||
[[Category: Blanot, D.]] | [[Category: Blanot, D.]] | ||
[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
[[Category: Fanchon, E.]] | [[Category: Fanchon, E.]] | ||
| - | [[Category: Heijenoort, J | + | [[Category: Heijenoort, J Van.]] |
[[Category: Martin, L.]] | [[Category: Martin, L.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:42 2008'' |
Revision as of 17:14, 21 February 2008
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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 with , and as ligands. Active as UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase, with EC number 6.3.2.9 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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