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Structure paper

TitleUnderstanding GFP Chromophore Biosynthesis: Controlling Backbone Cyclization and Modifying Post-translational Chemistry.
Journal, issue, pagesBiochemistry, Vol. 44, Page 1960-1970, Year 2005
Publish dateJan 7, 2005 (structure data deposition date)
AuthorsBarondeau, D.P. / Kassmann, C.J. / Tainer, J.A. / Getzoff, E.D.
External linksBiochemistry / PubMed:15697221
MethodsX-ray diffraction
Resolution1.35 - 2.5 Å
Structure data

PDB-1yhg:
Uncyclized precursor structure of S65G Y66S V68G GFP variant
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1yhh:
Uncyclized precursor structure of S65A Y66S G67A GFP variant
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-1yhi:
Uncyclized precursor structure of S65A Y66S R96A GFP variant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1yj2:
Cyclized, non-dehydrated post-translational product for S65A Y66S H148G GFP variant
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-1yjf:
Cyclized post-translational product for S65A Y66S (GFPhal) green fluorescent protein variant
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • aequorea victoria (jellyfish)
KeywordsLUMINESCENT PROTEIN / chromophore uncyclized dimer / Chromophore / uncyclized / coil-to-helix / MIO / electrophile / histidine / ammonia / lyase / HAL / biosynthesis / histidine ammonia lyase / design

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