View source for 7sqc


==Ciliary C1 central pair apparatus isolated from Chlamydomonas reinhardtii==
<StructureSection load='7sqc' size='340' side='right'caption='[[7sqc]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7sqc]] is a 63 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SQC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7sqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sqc OCA], [https://pdbe.org/7sqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sqc RCSB], [https://www.ebi.ac.uk/pdbsum/7sqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sqc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8I439_CHLRE A8I439_CHLRE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules are patterned asymmetrically with large protein complexes that repeat every 16 or 32 nm. The composition of these projections and the mechanisms that establish asymmetry and longitudinal periodicity are unknown. Here, by determining cryo-EM structures of the CA microtubules, we identify 48 different CA-associated proteins, which in turn reveal mechanisms for asymmetric and periodic protein binding to microtubules. We identify arc-MIPs, a novel class of microtubule inner protein, that bind laterally across protofilaments and remodel tubulin structure and lattice contacts. The binding mechanisms utilized by CA proteins may be generalizable to other microtubule-associated proteins. These structures establish a foundation to elucidate the contributions of individual CA proteins to ciliary motility and ciliopathies.

Ciliary central apparatus structure reveals mechanisms of microtubule patterning.,Gui M, Wang X, Dutcher SK, Brown A, Zhang R Nat Struct Mol Biol. 2022 May;29(5):483-492. doi: 10.1038/s41594-022-00770-2. , Epub 2022 May 16. PMID:35578023<ref>PMID:35578023</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sqc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Brown A]]
[[Category: Dutcher SK]]
[[Category: Gui M]]
[[Category: Wang X]]
[[Category: Zhang R]]