1r7h
From Proteopedia
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'''NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer''' | '''NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer''' | ||
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[[Category: Lindqvist, Y.]] | [[Category: Lindqvist, Y.]] | ||
[[Category: Stehr, M.]] | [[Category: Stehr, M.]] | ||
| - | [[Category: | + | [[Category: Domain swapping]] |
| - | [[Category: | + | [[Category: Glutaredoxin]] |
| - | [[Category: | + | [[Category: Nrdh]] |
| - | [[Category: | + | [[Category: Redox protein]] |
| - | [[Category: | + | [[Category: Thioredoxin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:10:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:10, 3 May 2008
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 Page seeded by OCA on Sat May 3 07:10:58 2008
