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| | <StructureSection load='1r7h' size='340' side='right'caption='[[1r7h]], [[Resolution|resolution]] 2.69Å' scene=''> | | <StructureSection load='1r7h' size='340' side='right'caption='[[1r7h]], [[Resolution|resolution]] 2.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r7h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_ammoniagenes"_cooke_and_keith_1927 "bacterium ammoniagenes" cooke and keith 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R7H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R7H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r7h]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R7H FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nrdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1697 "Bacterium ammoniagenes" Cooke and Keith 1927])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r7h OCA], [http://pdbe.org/1r7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r7h RCSB], [http://www.ebi.ac.uk/pdbsum/1r7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r7h ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r7h OCA], [https://pdbe.org/1r7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r7h RCSB], [https://www.ebi.ac.uk/pdbsum/1r7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r7h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O69271_CORAM O69271_CORAM] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium ammoniagenes cooke and keith 1927]] | + | [[Category: Corynebacterium ammoniagenes]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lindqvist, Y]] | + | [[Category: Lindqvist Y]] |
| - | [[Category: Stehr, M]] | + | [[Category: Stehr M]] |
| - | [[Category: Domain swapping]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Glutaredoxin]]
| + | |
| - | [[Category: Nrdh]]
| + | |
| - | [[Category: Redox protein]]
| + | |
| - | [[Category: Thioredoxin]]
| + | |
| Structural highlights
Function
O69271_CORAM
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer.,Stehr M, Lindqvist Y Proteins. 2004 May 15;55(3):613-9. PMID:15103625[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stehr M, Lindqvist Y. NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer. Proteins. 2004 May 15;55(3):613-9. PMID:15103625 doi:10.1002/prot.20126
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