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==== | ==Structure of the CatSpermasome== | ||
<StructureSection load='7eeb' size='340' side='right'caption='[[7eeb]]' scene=''> | <StructureSection load='7eeb' size='340' side='right'caption='[[7eeb]], [[Resolution|resolution]] 2.90Å' 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'>[[7eeb]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betaherpesvirus_5 Human betaherpesvirus 5] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EEB 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=7eeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eeb OCA], [https://pdbe.org/7eeb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eeb RCSB], [https://www.ebi.ac.uk/pdbsum/7eeb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eeb ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9Z9:(3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en'>9Z9</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7eeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eeb OCA], [https://pdbe.org/7eeb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eeb RCSB], [https://www.ebi.ac.uk/pdbsum/7eeb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eeb ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cation channel of sperm (CatSper) is essential for sperm motility and fertility(1,2). CatSper comprises the pore-forming proteins CATSPER1-4 and multiple auxiliary subunits, including CATSPERbeta, gamma, delta, epsilon, zeta, and EFCAB9(1,3-9). Here we report the cryo-electron microscopy (cryo-EM) structure of the CatSper complex isolated from mouse sperm. In the extracellular view, CATSPER1-4 conform to the conventional domain-swapped voltage-gated ion channel fold(10), following a counterclockwise arrangement. The auxiliary subunits CATSPERbeta, gamma, delta and epsilon-each of which contains a single transmembrane segment and a large extracellular domain-constitute a pavilion-like structure that stabilizes the entire complex through interactions with CATSPER4, 1, 3 and 2, respectively. Our EM map reveals several previously uncharacterized components, exemplified by the organic anion transporter SLCO6C1. We name this channel-transporter ultracomplex the CatSpermasome. The assembly and organization details of the CatSpermasome presented here lay the foundation for the development of CatSpermasome-related treatments for male infertility and non-hormonal contraceptives. | |||
Structure of a mammalian sperm cation channel complex.,Lin S, Ke M, Zhang Y, Yan Z, Wu J Nature. 2021 Jul;595(7869):746-750. doi: 10.1038/s41586-021-03742-6. Epub 2021 , Jul 5. PMID:34225353<ref>PMID:34225353</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7eeb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human betaherpesvirus 5]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Ke M]] | |||
[[Category: Wu JP]] | |||
Latest revision as of 12:24, 9 October 2024
Structure of the CatSpermasomeStructure of the CatSpermasome
Structural highlights
Publication Abstract from PubMedThe cation channel of sperm (CatSper) is essential for sperm motility and fertility(1,2). CatSper comprises the pore-forming proteins CATSPER1-4 and multiple auxiliary subunits, including CATSPERbeta, gamma, delta, epsilon, zeta, and EFCAB9(1,3-9). Here we report the cryo-electron microscopy (cryo-EM) structure of the CatSper complex isolated from mouse sperm. In the extracellular view, CATSPER1-4 conform to the conventional domain-swapped voltage-gated ion channel fold(10), following a counterclockwise arrangement. The auxiliary subunits CATSPERbeta, gamma, delta and epsilon-each of which contains a single transmembrane segment and a large extracellular domain-constitute a pavilion-like structure that stabilizes the entire complex through interactions with CATSPER4, 1, 3 and 2, respectively. Our EM map reveals several previously uncharacterized components, exemplified by the organic anion transporter SLCO6C1. We name this channel-transporter ultracomplex the CatSpermasome. The assembly and organization details of the CatSpermasome presented here lay the foundation for the development of CatSpermasome-related treatments for male infertility and non-hormonal contraceptives. Structure of a mammalian sperm cation channel complex.,Lin S, Ke M, Zhang Y, Yan Z, Wu J Nature. 2021 Jul;595(7869):746-750. doi: 10.1038/s41586-021-03742-6. Epub 2021 , Jul 5. PMID:34225353[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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