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''' | ==Structure of a fusion protein with a helix linker, 2ARH-3-3KAW-1.0== | ||
<StructureSection load='4zsv' size='340' side='right' caption='[[4zsv]], [[Resolution|resolution]] 4.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zsv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZSV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZSV FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zsx|4zsx]], [[4zsz|4zsz]]</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=4zsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zsv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zsv RCSB], [http://www.ebi.ac.uk/pdbsum/4zsv PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Connecting proteins together in prescribed geometric arrangements is an important element in new areas of biomolecular design. In this study, we characterize the degree of three-dimensional orientational control that can be achieved when two protein domains that have alpha-helical termini are joined using an alpha-helical linker. A fusion between naturally oligomeric protein domains was designed in this fashion with the intent of creating a self-assembling 12-subunit tetrahedral protein cage. While the designed fusion protein failed to assemble into a tetrahedral cage in high yield, a series of crystal structures showed that the two fused components were indeed bridged by an intact alpha helix, although the fusion protein was distorted from the intended ideal configuration by bending of the helix, ranging from 7 to 35 degrees . That range of deviation in orientation creates challenges for designing large, perfectly symmetric protein assemblies, although it should offer useful outcomes for other less geometrically demanding applications in synthetic biology. | |||
On the predictability of the orientation of protein domains joined by a spanning alpha-helical linker.,Lai YT, Jiang L, Chen W, Yeates TO Protein Eng Des Sel. 2015 Aug 4. pii: gzv035. PMID:26243886<ref>PMID:26243886</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Lai, Y T]] | |||
[[Category: Yeates, T O]] | |||
[[Category: Biomaterial]] | |||
[[Category: Bionanotechnology]] | |||
[[Category: Protein assembly]] | |||
[[Category: Protein design]] | |||
[[Category: Symmetry]] | |||
[[Category: Unknown function]] |
Revision as of 15:18, 20 August 2015
Structure of a fusion protein with a helix linker, 2ARH-3-3KAW-1.0Structure of a fusion protein with a helix linker, 2ARH-3-3KAW-1.0
Structural highlights
Publication Abstract from PubMedConnecting proteins together in prescribed geometric arrangements is an important element in new areas of biomolecular design. In this study, we characterize the degree of three-dimensional orientational control that can be achieved when two protein domains that have alpha-helical termini are joined using an alpha-helical linker. A fusion between naturally oligomeric protein domains was designed in this fashion with the intent of creating a self-assembling 12-subunit tetrahedral protein cage. While the designed fusion protein failed to assemble into a tetrahedral cage in high yield, a series of crystal structures showed that the two fused components were indeed bridged by an intact alpha helix, although the fusion protein was distorted from the intended ideal configuration by bending of the helix, ranging from 7 to 35 degrees . That range of deviation in orientation creates challenges for designing large, perfectly symmetric protein assemblies, although it should offer useful outcomes for other less geometrically demanding applications in synthetic biology. On the predictability of the orientation of protein domains joined by a spanning alpha-helical linker.,Lai YT, Jiang L, Chen W, Yeates TO Protein Eng Des Sel. 2015 Aug 4. pii: gzv035. PMID:26243886[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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