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Structure paper

TitleHelicobacter pylori periplasmic receptor CeuE (HP1561) modulates its nickel affinity via organic metallophores.
Journal, issue, pagesMol. Microbiol., Vol. 91, Page 724-735, Year 2014
Publish dateJan 5, 2013 (structure data deposition date)
AuthorsShaik, M.M. / Cendron, L. / Salamina, M. / Ruzzene, M. / Zanotti, G.
External linksMol. Microbiol. / PubMed:24330328
MethodsX-ray diffraction
Resolution1.65 - 2.3 Å
Structure data

PDB-4ino:
The crystal structure of Helicobacter pylori Ceue (HP1561)
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-4inp:
The crystal structure of Helicobacter pylori Ceue (HP1561) with Ni(II) bound
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4ls3:
THE crystal STRUCTURE OF HELICOBACTER PYLORI CEUE(HP1561)/NI-HIS COMPL
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NI:
NICKEL (II) ION

ChemComp-ACT:
ACETATE ION

ChemComp-HIS:
HISTIDINE

Source
  • helicobacter pylori (bacteria)
KeywordsTRANSPORT PROTEIN / heme-binding protein / Fe transport / ABC transporter substrate binding protein / periplasmic space / ABC TRANSPORTER / Rossmann-like fold / Ni binding

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