6r60: Difference between revisions

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'''Unreleased structure'''


The entry 6r60 is ON HOLD
==asymmetric antiparallel assembly of two 5-bladed beta-propeller fragments==
<StructureSection load='6r60' size='340' side='right'caption='[[6r60]], [[Resolution|resolution]] 1.75&Aring;' 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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

6r60, resolution 1.75Å

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