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1h75

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[[Image:1h75.gif|left|200px]]<br /><applet load="1h75" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h75.gif|left|200px]]
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caption="1h75, resolution 1.7&Aring;" />
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'''STRUCTURAL BASIS FOR THE THIOREDOXIN-LIKE ACTIVITY PROFILE OF THE GLUTAREDOXIN-LIKE PROTEIN NRDH-REDOXIN FROM ESCHERICHIA COLI.'''<br />
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{{Structure
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|PDB= 1h75 |SIZE=350|CAPTION= <scene name='initialview01'>1h75</scene>, resolution 1.7&Aring;
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|SITE= <scene name='pdbsite=DIS:Redox-Active+Disulfide'>DIS</scene>
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURAL BASIS FOR THE THIOREDOXIN-LIKE ACTIVITY PROFILE OF THE GLUTAREDOXIN-LIKE PROTEIN NRDH-REDOXIN FROM ESCHERICHIA COLI.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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]. Known structural/functional Site: <scene name='pdbsite=DIS:Redox-Active+Disulfide'>DIS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H75 OCA].
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1H75 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=1H75 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11441020 11441020]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11441020 11441020]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thioredoxin]]
[[Category: thioredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:33:12 2008''

Revision as of 09:33, 20 March 2008


PDB ID 1h75

Drag the structure with the mouse to rotate
, resolution 1.7Å
Sites:
Coordinates: save as pdb, mmCIF, xml



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. 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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