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Structure paper

TitleCrystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein.
Journal, issue, pagesBiochemistry, Vol. 47, Page 13004-13015, Year 2008
Publish dateJan 19, 2009 (structure data deposition date)
AuthorsSarma, R. / Barney, B.M. / Hamilton, T.L. / Jones, A. / Seefeldt, L.C. / Peters, J.W.
External linksBiochemistry / PubMed:19006326
MethodsX-ray diffraction
Resolution1.63 Å
Structure data

PDB-3fwy:
Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-HOH:
WATER

Source
  • rhodobacter sphaeroides 2.4.1 (bacteria)
KeywordsOXIDOREDUCTASE / BchL / protochlorophyllide / Electron donor / DPOR / Fe protein / nitrogenase / mixed alpha-beta domain / MgADP / ATP-binding / Bacteriochlorophyll biosynthesis / Chlorophyll biosynthesis / Iron / Iron-sulfur / Metal-binding / Nucleotide-binding / Photosynthesis

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