1e4e

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|PDB= 1e4e |SIZE=350|CAPTION= <scene name='initialview01'>1e4e</scene>, resolution 2.5&Aring;
|PDB= 1e4e |SIZE=350|CAPTION= <scene name='initialview01'>1e4e</scene>, resolution 2.5&Aring;
|SITE= <scene name='pdbsite=AC1:Phy+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Phy+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Adp+Binding+Site+For+Chain+A'>AC3</scene> and <scene name='pdbsite=AC4:Adp+Binding+Site+For+Chain+B'>AC4</scene>
|SITE= <scene name='pdbsite=AC1:Phy+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Phy+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Adp+Binding+Site+For+Chain+A'>AC3</scene> and <scene name='pdbsite=AC4:Adp+Binding+Site+For+Chain+B'>AC4</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PHY:1(S)-AMINOETHYL-(2-CARBOXYPROPYL)PHOSPHORYL-PHOSPHINIC+ACID'>PHY</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PHY:1(S)-AMINOETHYL-(2-CARBOXYPROPYL)PHOSPHORYL-PHOSPHINIC+ACID'>PHY</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= VANA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 Enterococcus faecium])
|GENE= VANA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 Enterococcus faecium])
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[[Category: plasmid]]
[[Category: plasmid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:49:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:36:18 2008''

Revision as of 09:36, 23 March 2008

Image:1e4e.jpg


PDB ID 1e4e

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites: , , and
Ligands: , , , and
Gene: VANA (Enterococcus faecium)
Coordinates: save as pdb, mmCIF, xml



D-ALANYL-D-LACATE LIGASE


Overview

d-alanine-d-lactate ligase from Enterococcus faecium BM4147 is directly responsible for the biosynthesis of alternate cell-wall precursors in bacteria, which are resistant to the glycopeptide antibiotic vancomycin. The crystal structure has been determined with data extending to 2.5-A resolution. This structure shows that the active site has unexpected interactions and is distinct from previous models for d-alanyl-d-lactate ligase mechanistic studies. It appears that the preference of the enzyme for lactate as a ligand over d-alanine could be mediated by electrostatic effects and/or a hydrogen-bonding network, which principally involve His-244. The structure of d-alanyl-d-lactate ligase provides a revised interpretation of the molecular events that lead to vancomycin resistance.

About this Structure

1E4E is a Protein complex structure of sequences from Enterococcus faecium. Full crystallographic information is available from OCA.

Reference

The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA)., Roper DI, Huyton T, Vagin A, Dodson G, Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8921-5. PMID:10908650

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