1rcf
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(New page: 200px<br /><applet load="1rcf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rcf, resolution 1.40Å" /> '''STRUCTURE OF THE TRI...)
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Revision as of 23:20, 20 November 2007
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STRUCTURE OF THE TRIGONAL FORM OF RECOMBINANT OXIDIZED FLAVODOXIN FROM ANABAENA 7120 AT 1.40 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1RCF is a Single protein structure of sequence from Anabaena sp. with SO4 and FMN as ligands. Full crystallographic information is available from OCA.
Reference
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
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