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- Title
Crystal Structure of Dimeric Flavodoxin from Desulfovibrio gigas Suggests a Potential Binding Region for the Electron-Transferring Partner.
- Authors
Yin-Cheng Hsieh; Tze Shyang Chia; Hoong-Kun Fun; Chun-Jung Chen
- Abstract
Flavodoxins, which exist widely in microorganisms, have been found in various pathways with multiple physiological functions. The flavodoxin (Fld) containing the cofactor flavin mononucleotide (FMN) from sulfur-reducing bacteria Desulfovibrio gigas (D. gigas) is a short-chain enzyme that comprises 146 residues with a molecular mass of 15 kDa and plays important roles in the electron-transfer chain. To investigate its structure, we purified this Fld directly from anaerobically grown D. gigas cells. The crystal structure of Fld, determined at resolution 1.3 Å, is a dimer with two FMN packing in an orientation head to head at a distance of 17 Å, which generates a long and connected negatively charged region. Two loops, Thr59-Asp63 and Asp95-Tyr100, are located in the negatively charged region and between two FMN, and are structurally dynamic. An analysis of each monomer shows that the structure of Fld is in a semiquinone state; the positions of FMN and the surrounding residues in the active site deviate. The crystal structure of Fld from D. gigas agrees with a dimeric form in the solution state. The dimerization area, dynamic characteristics and structure variations between monomers enable us to identify a possible binding area for its functional partners.
- Subjects
CRYSTAL structure; DIMERS; FLAVODOXIN; DESULFOVIBRIO; CHARGE exchange; BINDING sites; MONOMERS; NUCLEOTIDES
- Publication
International Journal of Molecular Sciences, 2013, Vol 14, Issue 1, p1667
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms14011667