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1h75
From Proteopedia
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==Overview== | ==Overview== | ||
| - | NrdH-redoxin is a representative of a class of small redox proteins that, contain a conserved CXXC motif and are characterized by a, glutaredoxin-like amino acid sequence and thioredoxin-like activity, profile. The crystal structure of recombinant Escherichia coli, NrdH-redoxin in the oxidized state has been determined at 1.7 A resolution, by multiwavelength anomalous diffraction. NrdH-redoxin belongs to the, thioredoxin superfamily and is structurally most similar to E. coli, glutaredoxin 3 and phage T4 glutaredoxin. The angle between the C-terminal, helix alpha3 and strand beta4, which differs between thioredoxin and, glutaredoxin, has an intermediate value in NrdH-redoxin. The orientation, of this helix is to a large extent determined by an extended hydrogen-bond, network involving the ... | + | NrdH-redoxin is a representative of a class of small redox proteins that, contain a conserved CXXC motif and are characterized by a, glutaredoxin-like amino acid sequence and thioredoxin-like activity, profile. The crystal structure of recombinant Escherichia coli, NrdH-redoxin in the oxidized state has been determined at 1.7 A resolution, by multiwavelength anomalous diffraction. NrdH-redoxin belongs to the, thioredoxin superfamily and is structurally most similar to E. coli, glutaredoxin 3 and phage T4 glutaredoxin. The angle between the C-terminal, helix alpha3 and strand beta4, which differs between thioredoxin and, glutaredoxin, has an intermediate value in NrdH-redoxin. The orientation, of this helix is to a large extent determined by an extended hydrogen-bond, network involving the highly conserved sequence motif (61)WSGFRP(D/E)(67), which is unique to this subclass of the thioredoxin superfamily. Residues, that bind glutathione in glutaredoxins are in general not conserved in, NrdH-redoxin, and no glutathione-binding cleft is present. Instead, NrdH-redoxin contains a wide hydrophobic pocket at the surface, similar to, thioredoxin. Modeling studies suggest that NrdH-redoxin can interact with, E. coli thioredoxin reductase at this pocket and also via a loop that is, complementary to a crevice in the reductase in a similar manner as, observed in the E. coli thioredoxin-thioredoxin reductase complex. |
==About this Structure== | ==About this Structure== | ||
| - | 1H75 is a | + | 1H75 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Structure known Active Site: DIS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H75 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:33:35 2007'' |
Revision as of 10:28, 5 November 2007
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STRUCTURAL BASIS FOR THE THIOREDOXIN-LIKE ACTIVITY PROFILE OF THE GLUTAREDOXIN-LIKE PROTEIN NRDH-REDOXIN FROM ESCHERICHIA COLI.
Overview
NrdH-redoxin is a representative of a class of small redox proteins that, contain a conserved CXXC motif and are characterized by a, glutaredoxin-like amino acid sequence and thioredoxin-like activity, profile. The crystal structure of recombinant Escherichia coli, NrdH-redoxin in the oxidized state has been determined at 1.7 A resolution, by multiwavelength anomalous diffraction. NrdH-redoxin belongs to the, thioredoxin superfamily and is structurally most similar to E. coli, glutaredoxin 3 and phage T4 glutaredoxin. The angle between the C-terminal, helix alpha3 and strand beta4, which differs between thioredoxin and, glutaredoxin, has an intermediate value in NrdH-redoxin. The orientation, of this helix is to a large extent determined by an extended hydrogen-bond, network involving the highly conserved sequence motif (61)WSGFRP(D/E)(67), which is unique to this subclass of the thioredoxin superfamily. Residues, that bind glutathione in glutaredoxins are in general not conserved in, NrdH-redoxin, and no glutathione-binding cleft is present. Instead, NrdH-redoxin contains a wide hydrophobic pocket at the surface, similar to, thioredoxin. Modeling studies suggest that NrdH-redoxin can interact with, E. coli thioredoxin reductase at this pocket and also via a loop that is, complementary to a crevice in the reductase in a similar manner as, observed in the E. coli thioredoxin-thioredoxin reductase complex.
About this Structure
1H75 is a Single protein structure of sequence from Escherichia coli. Structure known Active Site: DIS. Full crystallographic information is available from OCA.
Reference
Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coli., Stehr M, Schneider G, Aslund F, Holmgren A, Lindqvist Y, J Biol Chem. 2001 Sep 21;276(38):35836-41. Epub 2001 Jul 5. PMID:11441020
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