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Structure paper

TitleAllosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies.
Journal, issue, pagesProc. Natl. Acad. Sci. Usa, Vol. 103, Page 15178-15183, Year 2006
Publish dateAug 31, 2006 (structure data deposition date)
AuthorsLiu, S. / Chang, J.S. / Herberg, J.T. / Horng, M.M. / Tomich, P.K. / Lin, A.H. / Marotti, K.R.
External linksProc. Natl. Acad. Sci. Usa / PubMed:17015835
MethodsX-ray diffraction
Resolution2 - 2.46 Å
Structure data

PDB-2i80:
Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies
Method: X-RAY DIFFRACTION / Resolution: 2.19 Å

PDB-2i87:
Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2i8c:
Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies
Method: X-RAY DIFFRACTION / Resolution: 2.46 Å

Chemicals

ChemComp-G1L:
3-CHLORO-2,2-DIMETHYL-N-[4-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • staphylococcus aureus (bacteria)
  • staphylococcus aureus subsp. aureus (bacteria)
KeywordsLIGASE / protein-inhibitor complex / d-alanine:d-alanine ligase / apo / LYASE / ADP complex / Staphylococcus aureus

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