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| - | [[Image:1r7h.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1r7h| PDB=1r7h | SCENE= }} | | {{STRUCTURE_1r7h| PDB=1r7h | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15103625}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15103625 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15103625}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Redox protein]] | | [[Category: Redox protein]] |
| | [[Category: Thioredoxin]] | | [[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 Tue Jul 29 06:02:51 2008'' |
Revision as of 03:03, 29 July 2008
Template:STRUCTURE 1r7h
NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer
Template:ABSTRACT PUBMED 15103625
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 Tue Jul 29 06:02:51 2008
