4iwb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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. | [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;"> | ||
| - | == 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4iwb" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Flagellin 3D structures|Flagellin 3D structures]] | *[[Flagellin 3D structures|Flagellin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Novel Fold of FliC/FliS Fusion Protein
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