1e8c
From Proteopedia
(New page: 200px<br /><applet load="1e8c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e8c, resolution 2.00Å" /> '''STRUCTURE OF MURE TH...) |
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| - | [[Image:1e8c.gif|left|200px]]<br /><applet load="1e8c" size=" | + | [[Image:1e8c.gif|left|200px]]<br /><applet load="1e8c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e8c, resolution 2.00Å" /> | caption="1e8c, resolution 2.00Å" /> | ||
'''STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI'''<br /> | '''STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a | + | UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a cytoplasmic enzyme that catalyzes the addition of meso-diaminopimelic acid to nucleotide precursor UDP-N-acetylmuramoyl-l-alanyl-d-glutamate in the biosynthesis of bacterial cell-wall peptidoglycan. The crystal structure of the Escherichia coli enzyme in the presence of the final product of the enzymatic reaction, UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, has been solved to 2.0 A resolution. Phase information was obtained by multiwavelength anomalous dispersion using the K shell edge of selenium. The protein consists of three domains, two of which have a topology reminiscent of the equivalent domain found in the already established three-dimensional structure of the UDP-N-acetylmuramoyl-l-alanine: D-glutamate-ligase (MurD) ligase, which catalyzes the immediate previous step of incorporation of d-glutamic acid in the biosynthesis of the peptidoglycan precursor. The refined model reveals the binding site for UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, and comparison with the six known MurD structures allowed the identification of residues involved in the enzymatic mechanism. Interestingly, during refinement, an excess of electron density was observed, leading to the conclusion that, as in MurD, a carbamylated lysine residue is present in the active site. In addition, the structural determinant responsible for the selection of the amino acid to be added to the nucleotide precursor was identified. |
==About this Structure== | ==About this Structure== | ||
| - | 1E8C 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 CL and UAG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1E8C 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=CL:'>CL</scene> and <scene name='pdbligand=UAG:'>UAG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chantala, L.]] | [[Category: Chantala, L.]] | ||
[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
| - | [[Category: Gordon, E | + | [[Category: Gordon, E J.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: UAG]] | [[Category: UAG]] | ||
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[[Category: peptidoglycan biosynthesis]] | [[Category: peptidoglycan biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:58 2008'' |
Revision as of 10:25, 21 February 2008
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STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI
Overview
UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a cytoplasmic enzyme that catalyzes the addition of meso-diaminopimelic acid to nucleotide precursor UDP-N-acetylmuramoyl-l-alanyl-d-glutamate in the biosynthesis of bacterial cell-wall peptidoglycan. The crystal structure of the Escherichia coli enzyme in the presence of the final product of the enzymatic reaction, UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, has been solved to 2.0 A resolution. Phase information was obtained by multiwavelength anomalous dispersion using the K shell edge of selenium. The protein consists of three domains, two of which have a topology reminiscent of the equivalent domain found in the already established three-dimensional structure of the UDP-N-acetylmuramoyl-l-alanine: D-glutamate-ligase (MurD) ligase, which catalyzes the immediate previous step of incorporation of d-glutamic acid in the biosynthesis of the peptidoglycan precursor. The refined model reveals the binding site for UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, and comparison with the six known MurD structures allowed the identification of residues involved in the enzymatic mechanism. Interestingly, during refinement, an excess of electron density was observed, leading to the conclusion that, as in MurD, a carbamylated lysine residue is present in the active site. In addition, the structural determinant responsible for the selection of the amino acid to be added to the nucleotide precursor was identified.
About this Structure
1E8C is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli., Gordon E, Flouret B, Chantalat L, van Heijenoort J, Mengin-Lecreulx D, Dideberg O, J Biol Chem. 2001 Apr 6;276(14):10999-1006. Epub 2000 Dec 20. PMID:11124264
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