(2012). Crystal Structure of ChrR-A Quinone Reductase with the Capacity to Reduce Chromate. Plos One. 7 (4). e36017 (7p.). https://doi.org/10.1371/journal.pone.0036017, https://archimer.ifremer.fr/doc/00452/56372/
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Crystal Structure of ChrR-A Quinone Reductase with the Capacity to Reduce Chromate
The Escherichia coli ChrR enzyme is an obligatory two-electron quinone reductase that has many applications, such as in chromate bioremediation. Its crystal structure, solved at 2.2 angstrom resolution, shows that it belongs to the flavodoxin superfamily in which flavin mononucleotide (FMN) is firmly anchored to the protein. ChrR crystallized as a tetramer, and size exclusion chromatography showed that this is the oligomeric form that catalyzes chromate reduction. Within the tetramer, the dimers interact by a pair of two hydrogen bond networks, each involving Tyr128 and Glu146 of one dimer and Arg125 and Tyr85 of the other; the latter extends to one of the redox FMN cofactors. Changes in each of these amino acids enhanced chromate reductase activity of the enzyme, showing that this network is centrally involved in chromate reduction.
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Publisher's official version | 7 | 430 Ko | ||
Figure S1. The difference |Fo-Fc| map showing electron density compatible with flavin mononucleotide (FMN) prosthetic group. https://doi.org/10.1371/journal.pone.0036017.s001 | 1 | 248 Ko | ||
Figure S2. Structure of the ChrR dimer indicating the position of the calcium ion. https://doi.org/10.1371/journal.pone.0036017.s002 | 1 | 185 Ko | ||
Table S1. Primers used for site-directed mutagenesis. https://doi.org/10.1371/journal.pone.0036017.s003 | 1 | 63 Ko | ||
Table S2. Residues involved in dimer formation. https://doi.org/10.1371/journal.pone.0036017.s004 | 1 | 54 Ko | ||
Table S3. Distances of the hydrogen bonds (Å) presented in Figures 3 and 4. Residue name followed by (S) represents the symmetry related partner involved in the hydrogen bond. | 1 | 53 Ko |
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