3SVL
Structural basis of the improvement of ChrR - a multi-purpose enzyme
Summary for 3SVL
| Entry DOI | 10.2210/pdb3svl/pdb |
| Descriptor | protein yieF, FLAVIN MONONUCLEOTIDE, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | e. coli chrr enzyme, chromate bioremediation, tetramer role, improved mutant enzymes, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 42652.69 |
| Authors | Poulain, S.,Eswaramoorthy, S.,Hienerwadel, R.,Bremond, N.,Sylvester, M.D.,Zhang, Y.B.,Van Der Lelie, D.,Berthomieu, C.,Matin, A.C. (deposition date: 2011-07-12, release date: 2012-05-30, Last modification date: 2023-09-13) |
| Primary citation | Eswaramoorthy, S.,Poulain, S.,Hienerwadel, R.,Bremond, N.,Sylvester, M.D.,Zhang, Y.B.,Berthomieu, C.,Van Der Lelie, D.,Matin, A. Crystal Structure of ChrR-A Quinone Reductase with the Capacity to Reduce Chromate. Plos One, 7:e36017-e36017, 2012 Cited by PubMed Abstract: 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 Å 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. PubMed: 22558308DOI: 10.1371/journal.pone.0036017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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