6fc5: Difference between revisions
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New page: '''Unreleased structure''' The entry 6fc5 is ON HOLD Authors: Kumar, A., Stangier, M.M., Steinmetz, M.O. Description: Bik1 CAP-Gly domain Category: Unreleased Structures [[Category... |
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The | ==Bik1 CAP-Gly domain== | ||
<StructureSection load='6fc5' size='340' side='right'caption='[[6fc5]], [[Resolution|resolution]] 1.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fc5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FC5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88Å</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=6fc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fc5 OCA], [https://pdbe.org/6fc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fc5 RCSB], [https://www.ebi.ac.uk/pdbsum/6fc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fc5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BIK1_YEAST BIK1_YEAST] Required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. Probably required for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In budding yeast, the microtubule plus-end tracking proteins Bik1 (CLIP-170) and Bim1 (EB1) form a complex that interacts with partners involved in spindle positioning, including Stu2 and Kar9. Here, we show that the CAP-Gly and coiled-coil domains of Bik1 interact with the C-terminal ETF peptide of Bim1 and the C-terminal tail region of Stu2, respectively. The crystal structures of the CAP-Gly domain of Bik1 (Bik1CG) alone and in complex with an ETF peptide revealed unique, functionally relevant CAP-Gly elements, establishing Bik1CG as a specific C-terminal phenylalanine recognition domain. Unlike the mammalian CLIP-170-EB1 complex, Bik1-Bim1 forms ternary complexes with the EB1-binding motifs SxIP and LxxPTPh, which are present in diverse proteins, including Kar9. Perturbation of the Bik1-Bim1 interaction in vivo affected Bik1 localization and astral microtubule length. Our results provide insight into the role of the Bik1-Bim1 interaction for cell division, and demonstrate that the CLIP-170-EB1 module is evolutionarily flexible. | |||
Structure-Function Relationship of the Bik1-Bim1 Complex.,Stangier MM, Kumar A, Chen X, Farcas AM, Barral Y, Steinmetz MO Structure. 2018 Apr 3;26(4):607-618.e4. doi: 10.1016/j.str.2018.03.003. Epub 2018, Mar 22. PMID:29576319<ref>PMID:29576319</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Kumar | <div class="pdbe-citations 6fc5" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Kumar A]] | |||
[[Category: Stangier MM]] | |||
[[Category: Steinmetz MO]] | |||
