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

Replaces:  3END

Summary for 3FWY

• Entry DOI: 10.2210/pdb3fwy/pdb
• Descriptor: Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: 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, oxidoreductase, photosynthesis
• Biological source: Rhodobacter sphaeroides 2.4.1
• Total number of polymer chains: 2
• Total formula weight: 70284.74

Authors

Sarma, R.,Barney, B.M.,Hamilton, T.L.,Jones, A.,Seefeldt, L.C.,Peters, J.W. (deposition date: 2009-01-19, release date: 2009-03-24, Last modification date: 2023-09-06)

• Primary citation: Sarma, R.,Barney, B.M.,Hamilton, T.L.,Jones, A.,Seefeldt, L.C.,Peters, J.W.; Crystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein.; Biochemistry, 47:13004-13015, 2008; PubMed: 19006326; DOI: 10.1021/bi801058r

Experimental method

X-RAY DIFFRACTION (1.63 Å)