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Structure paper

TitleDistinct chromophore-protein environments enable asymmetric activation of a bacteriophytochrome-activated diguanylate cyclase.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 539-551, Year 2020
Publish dateJul 18, 2019 (structure data deposition date)
AuthorsBuhrke, D. / Gourinchas, G. / Muller, M. / Michael, N. / Hildebrandt, P. / Winkler, A.
External linksJ. Biol. Chem. / PubMed:31801828
MethodsX-ray diffraction
Resolution2.4 - 3 Å
Structure data

PDB-6saw:
Chromophore binding domain of bacteriophytochrome linked diguanylyl cyclase from Idiomarina species A28L (dimeric Pfr-like state).
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-6sax:
Chromophore binding domain of bacteriophytochrome linked diguanylyl cyclase from Idiomarina species A28L (Pr-state monomer).
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-LBV:
3-[2-[(Z)-[3-(2-carboxyethyl)-5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-4-methyl-pyrrol-1-ium

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • idiomarina sp. a28l (bacteria)
KeywordsLYASE / bacteriophytochrome / biliverdin / activated conformation / FLUORESCENT PROTEIN / monomer / protein

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