ArticleInternational journal of molecular sciences2013
Crystal structure of dimeric flavodoxin from Desulfovibrio gigas suggests a potential binding region for the electron-transferring partner.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 12 citations in OpenAlex.
- Effect of Dimer Structure and Inhomogeneous Broadening of Energy Levels on the Action of Flavomononucleotide in Rigid Polyvinyl Alcohol Films.International journal of molecular sciences · 2021Article
- Structure and function of an unusual flavodoxin from the domainProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Predicting Protein-Protein Interactions Using BiGGER: Case Studies.Molecules (Basel, Switzerland) · 2016Article
- WrpA Is an Atypical Flavodoxin Family Protein under Regulatory Control of the Brucella abortus General Stress Response System.Journal of bacteriology · 2016Article
- An Analysis of MIF Structural Features that Control Functional Activation of CD74.Chemistry & biology · 2015Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
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.
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