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Literature summary for 6.1.2.1 extracted from
- Molecular basis of vancomycin dependence in VanA-type Staphylococcus aureus VRSA-9 (2010), J. Bacteriol., 192, 5465-5471.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of C-terminally His6-tagged VRSA-9 Ddl | Staphylococcus aureus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| VRSA-9 Ddl X-ray diffraction crystal structure determination and analysis | Staphylococcus aureus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Q260K/A283E | the two amino acid substitutions result from point mutations at nucleotide positions 778 and 848, respectively. The mutant enzyme VRSA-9 synthesizes precursors ending in D-Ala-D-Lac (72%) and D-Ala-D-Ala (21%) in the absence of vancomycin. VRSA-9 Ddl shows a 200fold loss of activity and the importance of conformational changes in the dimer interface which can indirectly affect the topology of the active site | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Oxacillin | VRSA-9 Ddl is less sensitive than VRSA-6 Ddl | Staphylococcus aureus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Staphylococcus aureus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 41000 | - |
2 * 41000, recombinant C-terminally His6-tagged, SDS-PAGE | Staphylococcus aureus |
| 82000 | - |
recombinant C-terminally His6-tagged, gel filtration | Staphylococcus aureus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
- |
- |
| Staphylococcus aureus VRSA-9 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | ligand binding sites of VRSA-9 Ddl, overview | Staphylococcus aureus | ? | - |
? | |
| additional information | ligand binding sites of VRSA-9 Ddl, overview | Staphylococcus aureus VRSA-9 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 41000, recombinant C-terminally His6-tagged, SDS-PAGE | Staphylococcus aureus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| VRSA-9 Ddl | - |
Staphylococcus aureus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Staphylococcus aureus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the two amino acid substitutions Q260K/A283E via exchange at nucleotide positions 778 and 848, respectively, in VRSA-9 Ddl lead to the ability to synthesize precursors ending in D-Ala-D-Lac (72%) and D-Ala-D-Ala (21%) in the absence of vancomycin. The VRSA-9 Ddl has an altered D-Ala:D-Ala ligase activity relative to that of VRSA-6 with a Km for D-Ala of 2 mM at subsite 1 and 240 mM at subsite 2. The binding affinity for D-Ala at subsite 2 is 14fold lower than that of VRSA-6. The residues at nucleotide positions 778 and 848 are not conserved among D-Ala:DAla ligases and do not interact directly with the substrates. VRSA-9 Ddl shows the importance of conformational changes in the dimer interface which can indirectly affect the topology of the active site | Staphylococcus aureus |
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