1r7h
From Proteopedia
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| - | [[Image:1r7h.jpg|left|200px]] | + | [[Image:1r7h.jpg|left|200px]] |
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| - | '''NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer''' | + | {{Structure |
| + | |PDB= 1r7h |SIZE=350|CAPTION= <scene name='initialview01'>1r7h</scene>, resolution 2.69Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= nrdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1697 Corynebacterium ammoniagenes]) | ||
| + | }} | ||
| + | |||
| + | '''NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R7H is a [ | + | 1R7H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R7H OCA]. |
==Reference== | ==Reference== | ||
| - | NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer., Stehr M, Lindqvist Y, Proteins. 2004 May 15;55(3):613-9. PMID:[http:// | + | NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer., Stehr M, Lindqvist Y, Proteins. 2004 May 15;55(3):613-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103625 15103625] |
[[Category: Corynebacterium ammoniagenes]] | [[Category: Corynebacterium ammoniagenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''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 13:47:57 2008'' |
Revision as of 11:47, 20 March 2008
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| , resolution 2.69Å | |||||||
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| Gene: | nrdh (Corynebacterium ammoniagenes) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer
Overview
NrdH-redoxins constitute a family of small redox proteins, which contain a conserved CXXC sequence motif, and are characterized by a glutaredoxin-like amino acid sequence but a thioredoxin-like activity profile. Here we report the structure of Corynebacterium ammoniagenes NrdH at 2.7 A resolution, determined by molecular replacement using E. coli NrdH as model. The structure is the first example of a domain-swapped dimer from the thioredoxin family. The domain-swapped structure is formed by an inter-chain two-stranded anti-parallel beta-sheet and is stabilized by electrostatic interactions at the dimer interface. Size exclusion chromatography, and MALDI-ESI experiments revealed however, that the protein exists as a monomer in solution. Similar to E. coli NrdH-redoxin and thioredoxin, C. ammoniagenes NrdH-redoxin has a wide hydrophobic pocket at the surface that could be involved in binding to thioredoxin reductase. However, the loop between alpha2 and beta3, which is complementary to a crevice in the reductase in the thioredoxin-thioredoxin reductase complex, is the hinge for formation of the swapped dimer in C. ammoniagenes NrdH-redoxin. C. ammoniagenes NrdH-redoxin has the highly conserved sequence motif W61-S-G-F-R-P-[DE]67 which is unique to the NrdH-redoxins and which determines the orientation of helix alpha3. An extended hydrogen-bond network, similar to that in E. coli NrdH-redoxin, determines the conformation of the loop formed by the conserved motif.
About this Structure
1R7H is a Single protein structure of sequence from Corynebacterium ammoniagenes. Full crystallographic information is available from OCA.
Reference
NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer., Stehr M, Lindqvist Y, Proteins. 2004 May 15;55(3):613-9. PMID:15103625
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