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Structure paper

TitleIron-Coordinating Tyrosine Is a Key Determinant of NEAT Domain Heme Transfer.
Journal, issue, pagesJ. Mol. Biol., Vol. 413, Page 684-698, Year 2011
Publish dateMar 6, 2011 (structure data deposition date)
AuthorsGrigg, J.C. / Mao, C.X. / Murphy, M.E.
External linksJ. Mol. Biol. / PubMed:21893067
MethodsX-ray diffraction
Resolution1.25 - 2 Å
Structure data

PDB-3qzl:
Staphylococcus aureus IsdA NEAT domain K75A variant in complex with heme
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-3qzm:
Staphylococcus aureus IsdA NEAT domain H83A variant in complex with heme
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-3qzn:
Staphylococcus aureus IsdA NEAT domain Y166A variant in complex with heme
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3qzo:
Staphylococcus aureus IsdA NEAT domain in complex with heme, reduced crystal
Method: X-RAY DIFFRACTION / Resolution: 1.952 Å

PDB-3qzp:
Staphylococcus aureus IsdA NEAT domain in complex with cobalt-protoporphyrin IX
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-COH:
PROTOPORPHYRIN IX CONTAINING CO

Source
  • staphylococcus aureus subsp. aureus (bacteria)
KeywordsMETAL BINDING PROTEIN / heme / transport / iron / uptake / receptor / cell wall / ferrous

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