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Structure paper

TitleAdenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.
Journal, issue, pagesNature, Vol. 482, Page 107-110, Year 2012
Publish dateMay 25, 2011 (structure data deposition date)
AuthorsEngel, P. / Goepfert, A. / Stanger, F.V. / Harms, A. / Schmidt, A. / Schirmer, T. / Dehio, C.
External linksNature / PubMed:22266942
MethodsX-ray diffraction
Resolution1.5 - 3.03 Å
Structure data

PDB-3s6a:
Fic protein from NEISSERIA MENINGITIDIS in complex with AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3se5:
Fic protein from NEISSERIA MENINGITIDIS mutant delta8 in complex with AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3shg:
VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-3sn9:
Fic protein from NEISSERIA MENINGITIDIS mutant S182A/E186A in complex with AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 3.03 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-MG:
Unknown entry

ChemComp-TLA:
L(+)-TARTARIC ACID

Source
  • neisseria meningitidis (bacteria)
  • bartonella schoenbuchensis r1 (bacteria)
KeywordsTRANSFERASE / AMPylation / adenylylation / TRANSFERASE/PROTEIN BINDING / toxin-antitoxin complex / Fic fold / AMP transfer / TRANSFERASE-PROTEIN BINDING complex

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