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Structure paper

TitleOligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this family.
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 63, Page 361-368, Year 2007
Publish dateDec 2, 2005 (structure data deposition date)
AuthorsEzezika, O.C. / Haddad, S. / Neidle, E.L. / Momany, C.
External linksActa Crystallogr. ,Sect. F / PubMed:17565172
MethodsX-ray diffraction
Resolution2.2 - 2.7 Å
Structure data

PDB-2f8d:
BenM effector-Binding domain crystallized from high pH conditions
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-2f97:
Effector Binding Domain of BenM (crystals generated from high pH conditions)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-BEZ:
BENZOIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • acinetobacter baylyi (bacteria)
KeywordsGENE REGULATION / BenM / LTTR / LysR-type transcriptional regulator / tetramerization / Effector binding domain / Inducer binding domain / LysR-type regulator

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