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| | ==Novel Fold of FliC/FliS Fusion Protein== | | ==Novel Fold of FliC/FliS Fusion Protein== |
| - | <StructureSection load='4iwb' size='340' side='right' caption='[[4iwb]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='4iwb' size='340' side='right'caption='[[4iwb]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4iwb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IWB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4iwb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IWB FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ory|1ory]]</td></tr> | + | </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=4iwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iwb OCA], [https://pdbe.org/4iwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iwb RCSB], [https://www.ebi.ac.uk/pdbsum/4iwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iwb ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aq_1998, flaA, fliC, fliS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iwb OCA], [http://pdbe.org/4iwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4iwb RCSB], [http://www.ebi.ac.uk/pdbsum/4iwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4iwb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FLAA_AQUAE FLAA_AQUAE]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | + | [https://www.uniprot.org/uniprot/O67806_AQUAE O67806_AQUAE] [https://www.uniprot.org/uniprot/FLAA_AQUAE FLAA_AQUAE] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4iwb" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4iwb" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Flagellin 3D structures|Flagellin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquae]] | + | [[Category: Aquifex aeolicus]] |
| - | [[Category: Faham, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Motor protein]] | + | [[Category: Faham S]] |
| - | [[Category: Novel fold]]
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| Structural highlights
Function
O67806_AQUAE FLAA_AQUAE Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Publication Abstract from PubMed
Domain fusion is a useful tool in protein design. Here, the structure of a fusion of the heterodimeric flagella-assembly proteins FliS and FliC is reported. Although the ability of the fusion protein to maintain the structure of the heterodimer may be apparent, threading-based structural predictions do not properly fuse the heterodimer. Additional examples of naturally occurring heterodimers that are homologous to full-length proteins were identified. These examples highlight that the designed protein was engineered by the same tools as used in the natural evolution of proteins and that heterodimeric structures contain a wealth of information, currently unused, that can improve structural predictions.
Protein design by fusion: implications for protein structure prediction and evolution.,Skorupka K, Han SK, Nam HJ, Kim S, Faham S Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2451-60. doi:, 10.1107/S0907444913022701. Epub 2013 Nov 19. PMID:24311586[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Skorupka K, Han SK, Nam HJ, Kim S, Faham S. Protein design by fusion: implications for protein structure prediction and evolution. Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2451-60. doi:, 10.1107/S0907444913022701. Epub 2013 Nov 19. PMID:24311586 doi:http://dx.doi.org/10.1107/S0907444913022701
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