6zz8: Difference between revisions
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==== | ==MB_CRS6-15 bound to CrSAS-6_6HR== | ||
<StructureSection load='6zz8' size='340' side='right'caption='[[6zz8]]' scene=''> | <StructureSection load='6zz8' size='340' side='right'caption='[[6zz8]], [[Resolution|resolution]] 3.73Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[6zz8]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZ8 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=6zz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zz8 OCA], [https://pdbe.org/6zz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zz8 RCSB], [https://www.ebi.ac.uk/pdbsum/6zz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zz8 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]] 3.73Å</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=6zz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zz8 OCA], [https://pdbe.org/6zz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zz8 RCSB], [https://www.ebi.ac.uk/pdbsum/6zz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zz8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A9CQL4_CHLRE A9CQL4_CHLRE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Centrioles are evolutionarily conserved multi-protein organelles essential for forming cilia and centrosomes. Centriole biogenesis begins with self-assembly of SAS-6 proteins into 9-fold symmetrical ring polymers, which then stack into a cartwheel that scaffolds organelle formation. The importance of this architecture has been difficult to decipher notably because of the lack of precise tools to modulate the underlying assembly reaction. Here, we developed monobodies against Chlamydomonas reinhardtii SAS-6, characterizing three in detail with X-ray crystallography, atomic force microscopy and cryo-electron microscopy. This revealed distinct monobody-target interaction modes, as well as specific consequences on ring assembly and stacking. Of particular interest, monobody MB(CRS6)-15 induces a conformational change in CrSAS-6, resulting in the formation of a helix instead of a ring. Furthermore, we show that this alteration impairs centriole biogenesis in human cells. Overall, our findings identify monobodies as powerful molecular levers to alter the architecture of multi-protein complexes and tune centriole assembly. | |||
Tuning SAS-6 architecture with monobodies impairs distinct steps of centriole assembly.,Hatzopoulos GN, Kukenshoner T, Banterle N, Favez T, Fluckiger I, Hamel V, Andany S, Fantner GE, Hantschel O, Gonczy P Nat Commun. 2021 Jun 21;12(1):3805. doi: 10.1038/s41467-021-23897-0. PMID:34155202<ref>PMID:34155202</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6zz8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chlamydomonas reinhardtii]] | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Banterle N]] | ||
[[Category: Favez T]] | |||
[[Category: Fluckiger I]] | |||
[[Category: Gonczy P]] | |||
[[Category: Hantschel O]] | |||
[[Category: Hatzopoulos GN]] | |||
[[Category: Kukenshoner T]] | |||
Latest revision as of 15:00, 1 February 2024
MB_CRS6-15 bound to CrSAS-6_6HRMB_CRS6-15 bound to CrSAS-6_6HR
Structural highlights
FunctionPublication Abstract from PubMedCentrioles are evolutionarily conserved multi-protein organelles essential for forming cilia and centrosomes. Centriole biogenesis begins with self-assembly of SAS-6 proteins into 9-fold symmetrical ring polymers, which then stack into a cartwheel that scaffolds organelle formation. The importance of this architecture has been difficult to decipher notably because of the lack of precise tools to modulate the underlying assembly reaction. Here, we developed monobodies against Chlamydomonas reinhardtii SAS-6, characterizing three in detail with X-ray crystallography, atomic force microscopy and cryo-electron microscopy. This revealed distinct monobody-target interaction modes, as well as specific consequences on ring assembly and stacking. Of particular interest, monobody MB(CRS6)-15 induces a conformational change in CrSAS-6, resulting in the formation of a helix instead of a ring. Furthermore, we show that this alteration impairs centriole biogenesis in human cells. Overall, our findings identify monobodies as powerful molecular levers to alter the architecture of multi-protein complexes and tune centriole assembly. Tuning SAS-6 architecture with monobodies impairs distinct steps of centriole assembly.,Hatzopoulos GN, Kukenshoner T, Banterle N, Favez T, Fluckiger I, Hamel V, Andany S, Fantner GE, Hantschel O, Gonczy P Nat Commun. 2021 Jun 21;12(1):3805. doi: 10.1038/s41467-021-23897-0. PMID:34155202[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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