1ger
From Proteopedia
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| - | [[Image:1ger.gif|left|200px]] | + | [[Image:1ger.gif|left|200px]] |
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| - | '''THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES''' | + | {{Structure |
| + | |PDB= 1ger |SIZE=350|CAPTION= <scene name='initialview01'>1ger</scene>, resolution 1.86Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GER is a [ | + | 1GER is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GER OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8061609 8061609] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Glutathione-disulfide reductase]] | [[Category: Glutathione-disulfide reductase]] | ||
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[[Category: oxidoreductase(flavoenzyme)]] | [[Category: oxidoreductase(flavoenzyme)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:22:04 2008'' |
Revision as of 09:22, 20 March 2008
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| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutathione-disulfide reductase, with EC number 1.8.1.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 11:22:04 2008
