1ger
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(New page: 200px<br /><applet load="1ger" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ger, resolution 1.86Å" /> '''THE STRUCTURE OF GLU...)
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Revision as of 13:52, 20 November 2007
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THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES
Overview
The crystal structure of the dimeric flavoenzyme glutathione reductase, from Escherichia coli was determined and refined to an R-factor of 16.8%, at 1.86 A resolution. The molecular 2-fold axis of the dimer is local but, very close to a possible crystallographic 2-fold axis; the slight, asymmetry could be rationalized from the packing contacts. The 2, crystallographically independent subunits of the dimer are virtually, identical, yielding no structural clue on possible cooperativity. The, structure was compared with the well-known structure of the homologous, enzyme from human erythrocytes with 52% sequence identity. Significant, differences were found at the dimer interface, where the human enzyme has, a disulfide bridge, whereas the E. coli enzyme has an antiparallel, beta-sheet connecting the subunits. The differences at the glutathione, binding site and in particular a deformation caused by a Leu-Ile exchange, indicate why the E. coli enzyme accepts trypanothione much better than the, human enzyme. The reported structure provides a frame for explaining, numerous published engineering results in detail and for guiding further, ones.
About this Structure
1GER is a Single protein structure of sequence from Escherichia coli with FAD as ligand. Active as Glutathione-disulfide reductase, with EC number 1.8.1.7 Full crystallographic information is available from OCA.
Reference
Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes., Mittl PR, Schulz GE, Protein Sci. 1994 May;3(5):799-809. PMID:8061609
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