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6r60
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==asymmetric antiparallel assembly of two 5-bladed beta-propeller fragments== | |
| + | <StructureSection load='6r60' size='340' side='right'caption='[[6r60]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6r60]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R60 FirstGlance]. <br> | ||
| + | </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=6r60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r60 OCA], [http://pdbe.org/6r60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r60 RCSB], [http://www.ebi.ac.uk/pdbsum/6r60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r60 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | beta-Propellers arise through the amplification of a supersecondary structure element called a blade. This process produces toroids of between four and twelve repeats, which are almost always arranged sequentially in a single polypeptide chain. We found that new propellers evolve continuously by amplification from single blades. We therefore investigated whether such nascent propellers can fold as homo-oligomers before they have been fully amplified within a single chain. One- to six-bladed building blocks derived from two seven-bladed WD40 propellers yielded stable homo-oligomers with six to nine blades, depending on the size of the building block. High-resolution structures for tetramers of two blades, trimers of three blades, and dimers of four and five blades, respectively, show structurally diverse propellers and include a novel fold, highlighting the inherent flexibility of the WD40 blade. Our data support the hypothesis that subdomain-sized fragments can provide structural versatility in the evolution of new proteins. | ||
| - | + | Structural diversity of oligomeric beta-propellers with different numbers of identical blades.,Afanasieva E, Chaudhuri I, Martin J, Hertle E, Ursinus A, Alva V, Hartmann MD, Lupas AN Elife. 2019 Oct 15;8. pii: 49853. doi: 10.7554/eLife.49853. PMID:31613220<ref>PMID:31613220</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6r60" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Afanasieva, E]] | ||
| + | [[Category: Hartmann, M D]] | ||
| + | [[Category: Lupas, A N]] | ||
| + | [[Category: Fragment amplification]] | ||
| + | [[Category: Protein design]] | ||
| + | [[Category: Protein evolution]] | ||
| + | [[Category: Repeat protein]] | ||
| + | [[Category: Unknown function]] | ||
| + | [[Category: Wd40]] | ||
Revision as of 11:11, 13 November 2019
asymmetric antiparallel assembly of two 5-bladed beta-propeller fragments
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