1ger
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ger |SIZE=350|CAPTION= <scene name='initialview01'>1ger</scene>, resolution 1.86Å | |PDB= 1ger |SIZE=350|CAPTION= <scene name='initialview01'>1ger</scene>, resolution 1.86Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ger FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ger OCA], [http://www.ebi.ac.uk/pdbsum/1ger PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ger RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Mittl, P R.E.]] | [[Category: Mittl, P R.E.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: FAD]] | ||
[[Category: oxidoreductase(flavoenzyme)]] | [[Category: oxidoreductase(flavoenzyme)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:42:30 2008'' |
Revision as of 17:42, 30 March 2008
| |||||||
| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutathione-disulfide reductase, with EC number 1.8.1.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 20:42:30 2008
