3svl | pdb_00003svl

Structural basis of the improvement of ChrR - a multi-purpose enzyme

spinqualitylabelsall models 3svl, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3svl is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, FMN Gene: yieF, b3713, JW3691 (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 A 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. Crystal Structure of ChrR-A Quinone Reductase with the Capacity to Reduce Chromate.,Eswaramoorthy S, Poulain S, Hienerwadel R, Bremond N, Sylvester MD, Zhang YB, Berthomieu C, Van Der Lelie D, Matin A PLoS One. 2012;7(4):e36017. Epub 2012 Apr 27. PMID:22558308 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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