4HEQ
The crystal structure of flavodoxin from Desulfovibrio gigas
Summary for 4HEQ
| Entry DOI | 10.2210/pdb4heq/pdb |
| Descriptor | Flavodoxin, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | electron transfer, cytoplasma, electron transport |
| Biological source | Desulfovibrio gigas |
| Total number of polymer chains | 2 |
| Total formula weight | 31875.17 |
| Authors | Hsieh, Y.C.,Chen, C.J. (deposition date: 2012-10-04, release date: 2013-01-30, Last modification date: 2024-03-20) |
| Primary citation | Hsieh, Y.C.,Chia, T.S.,Fun, H.K.,Chen, C.J. Crystal Structure of Dimeric Flavodoxin from Desulfovibrio gigas Suggests a Potential Binding Region for the Electron-Transferring Partner Int J Mol Sci, 14:1667-1683, 2013 Cited by PubMed 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. PubMed: 23322018DOI: 10.3390/ijms14011667 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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