1rcf

STRUCTURE OF THE TRIGONAL FORM OF RECOMBINANT OXIDIZED FLAVODOXIN FROM ANABAENA 7120 AT 1.40 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1rcf, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1rcf is a 1 chain structure with sequence from Anabaena 7120. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FLAV_NOSS1] Low-potential electron donor to a number of redox enzymes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The oxidized recombinant flavodoxin from the cyanobacterium Anabaena 7120 has been crystallized in a trigonal form. The recombinant protein has an identical primary structure to that purified directly from Anabaena, which functions as a substitute for ferredoxin in an iron-deficient environment for electron transfer from photosystem I to ferredoxin-NADP(+) reductase. X-ray data to 1.40 A were collected on a Siemens area detector. Of the 311 379 reflections collected, 36069 reflections were unique in space group P3(1)21 (a = 55.36, c = 102.59 A) with an R(merge) of 3.8%. The structure was solved by molecular replacement using coordinates from the wild-type monoclinic structure previously solved in this laboratory [Rao, Shaffie, Yu, Satyshur, Stockman & Markley (1992). Protein Sci. 1, 1413-1427]. The structure was refined with X-PLOR and SHELXL93 to a crystallographic R-factor of 13.9% for 32963 reflections with I> 2sigma(I). The final structure contains 2767 atoms including 31 flavin mononucleotide (FMN) atoms, 299 water molecules, and one sulfate ion. The protein is comprised of a central five-stranded beta-sheet surrounded by five helices and binds a single molecule of FMN at the C-terminus of the sheet. The trigonal protein structure and the crystal packing are compared with the monoclinic wild-type protein. Helix alpha3 in this structure is less distorted than in the monoclinic structure and shows additional hydrogen bonds in the N-terminal portion of the helix. The trigonal structure is extensively hydrogen bonded in three major areas with neighboring molecules compared with five regions in the monoclinic structure, but using significantly fewer hydrogen bonds to stabilize the lattice. There are several hydrogen bonds to the amide groups from water molecules several of which stabilize and extend the ends of the beta-sheet. Structure of the trigonal form of recombinant oxidized flavodoxin from Anabaena 7120 at 1.40 A resolution.,Burkhart BM, Ramakrishnan B, Yan H, Reedstrom RJ, Markley JL, Straus NA, Sundaralingam M Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):318-30. PMID:15299298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flavodoxin 3D structures

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