Structural highlights
Function
[FLAV_DESVH] Low-potential electron donor to a number of redox enzymes.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystallographic structure of an engineered flavodoxin mutant from Desulfovibrio vulgaris has been analysed. Site-directed mutagenesis was used to substitute serine 35 with a cysteine to provide a possible covalent linkage. The crystal structure of the semiquinone form of this mutant is similar to the corresponding oxidation state of the wild-type flavodoxin. Analysis of the structural changes reveals the interaction between N(5)H of the flavin and the carbonyl O atom of Gly61 to be critical for modulation of the electrochemical properties of the protein.
Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state.,Artali R, Marchini N, Meneghetti F, Cavazzini D, Cassetta A, Sassone C Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):481-4. Epub 2005, Mar 24. PMID:15805604[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Artali R, Marchini N, Meneghetti F, Cavazzini D, Cassetta A, Sassone C. Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state. Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):481-4. Epub 2005, Mar 24. PMID:15805604 doi:10.1107/S0907444905001502
