1ger: Difference between revisions

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[[Image:1ger.gif|left|200px]]
{{Seed}}
[[Image:1ger.png|left|200px]]


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{{STRUCTURE_1ger|  PDB=1ger  |  SCENE=  }}  
{{STRUCTURE_1ger|  PDB=1ger  |  SCENE=  }}  


'''THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES'''
===THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_8061609}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_8061609}}


==About this Structure==
==About this Structure==
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[[Category: Mittl, P R.E.]]
[[Category: Mittl, P R.E.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
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