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Structure paper

TitleStructural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.
Journal, issue, pagesSci Rep, Vol. 7, Page 40408-40408, Year 2017
Publish dateOct 21, 2015 (structure data deposition date)
AuthorsSviridova, E. / Rezacova, P. / Bondar, A. / Veverka, V. / Novak, P. / Schenk, G. / Svergun, D.I. / Kuta Smatanova, I. / Bumba, L.
External linksSci Rep / PubMed:28084396
MethodsX-ray diffraction
Resolution1.4 - 2.3 Å
Structure data

PDB-5edf:
Crystal structure of the selenomethionine-substituted iron-regulated protein FrpD from Neisseria meningitidis
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-5edj:
Crystal structure of the Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-NA:
Unknown entry

ChemComp-AZI:
AZIDE ION

ChemComp-HOH:
WATER

Source
  • neisseria meningitidis (bacteria)
  • neisseria meningitidis mc58 (bacteria)
KeywordsUNKNOWN FUNCTION / Selenomethionine-substituted iron-regulated protein FrpD / FrpC-binding protein / novel fold / metal transport / Iron-regulated protein FrpD / membrane protein

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