1RCF

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

1RCF の概要

• エントリーDOI: 10.2210/pdb1rcf/pdb
• 分子名称: FLAVODOXIN, SULFATE ION, FLAVIN MONONUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: electron transfer(flavoprotein)
• 由来する生物種: Nostoc sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19399.94

構造登録者

Burkhart, B.,Ramakrishnan, B.,Yan, H.,Reedstrom, R.,Markley, J.,Straus, N.,Sundaralingam, M. (登録日: 1994-10-31, 公開日: 1995-01-26, 最終更新日: 2024-02-14)

主引用文献

Burkhart, B.M.,Ramakrishnan, B.,Yan, H.,Reedstrom, R.J.,Markley, J.L.,Straus, N.A.,Sundaralingam, M.
Structure of the trigonal form of recombinant oxidized flavodoxin from Anabaena 7120 at 1.40 A resolution.
Acta Crystallogr.,Sect.D, 51:318-330, 1995

PubMed Abstract: 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.

PubMed: 15299298
DOI: 10.1107/S0907444994011716

実験手法

X-RAY DIFFRACTION (1.4 Å)