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4iwb
From Proteopedia
(Difference between revisions)
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| - | + | ==Novel Fold of FliC/FliS Fusion Protein== | |
| - | + | <StructureSection load='4iwb' size='340' side='right' caption='[[4iwb]], [[Resolution|resolution]] 1.75Å' scene=''> | |
| - | + | == 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> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ory|1ory]]</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> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=4iwb RCSB], [http://www.ebi.ac.uk/pdbsum/4iwb PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24311586</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: Faham, S | + | </StructureSection> |
| + | [[Category: Aquae]] | ||
| + | [[Category: Faham, S]] | ||
[[Category: Motor protein]] | [[Category: Motor protein]] | ||
[[Category: Novel fold]] | [[Category: Novel fold]] | ||
Revision as of 18:55, 21 December 2014
Novel Fold of FliC/FliS Fusion Protein
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