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Structure paper

TitleDistinct Effector-binding Sites Enable Synergistic Transcriptional Activation by BenM, a LysR-type Regulator.
Journal, issue, pagesJ. Mol. Biol., Vol. 367, Page 616-629, Year 2007
Publish dateNov 29, 2005 (structure data deposition date)
AuthorsEzezika, O.C. / Haddad, S. / Clark, T.J. / Neidle, E.L. / Momany, C.
External linksJ. Mol. Biol. / PubMed:17291527
MethodsX-ray diffraction
Resolution1.9 - 2.162 Å
Structure data

PDB-2f6g:
BenM effector binding domain
Method: X-RAY DIFFRACTION / Resolution: 1.908 Å

PDB-2f6p:
BenM effector binding domain- SeMet derivative
Method: X-RAY DIFFRACTION / Resolution: 2.001 Å

PDB-2f78:
BenM effector binding domain with its effector benzoate
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-2f7a:
BenM effector binding domain with its effector, cis,cis-muconate
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2f7b:
CatM effector binding domain
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2f7c:
CatM effector binding domain with its effector cis,cis-muconate
Method: X-RAY DIFFRACTION / Resolution: 2.162 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

ChemComp-NA:
Unknown entry

ChemComp-BEZ:
BENZOIC ACID

ChemComp-CCU:
(2Z,4Z)-HEXA-2,4-DIENEDIOIC ACID

Source
  • acinetobacter baylyi (bacteria)
KeywordsTRANSCRIPTION / LTTR / lysR-type transcriptional regulator / inducer binding domain / effector binding domain / GENE REGULATION / muconate

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