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Structure paper

TitleThe Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 11162-11171, Year 2010
Publish dateJan 23, 2010 (structure data deposition date)
AuthorsGrigg, J.C. / Cooper, J.D. / Cheung, J. / Heinrichs, D.E. / Murphy, M.E.
External linksJ. Biol. Chem. / PubMed:20147287
MethodsX-ray diffraction
Resolution1.3 - 2.2 Å
Structure data

PDB-3lhs:
Open Conformation of HtsA Complexed with Staphyloferrin A
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-3li2:
Closed Conformation of HtsA Complexed with Staphyloferrin A
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-FE:
Unknown entry

ChemComp-SF8:
(2R)-2-(2-{[(1R)-1-carboxy-4-{[(3S)-3,4-dicarboxy-3-hydroxybutanoyl]amino}butyl]amino}-2-oxoethyl)-2-hydroxybutanedioic

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-ACT:
ACETATE ION

Source
  • staphylococcus aureus subsp. aureus strain (bacteria)
  • staphylococcus aureus subsp. aureus (bacteria)
KeywordsTRANSPORT PROTEIN / siderophore / iron / receptor / lipoprotein / binding protein

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