6f64: Difference between revisions
New page: '''Unreleased structure''' The entry 6f64 is ON HOLD until Paper Publication Authors: Dunce, J.M., Millan, C., Uson, I., Davies, O.R. Description: Crystal structure of the SYCP1 C-term... |
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==Crystal structure of the SYCP1 C-terminal back-to-back assembly== | |||
<StructureSection load='6f64' size='340' side='right'caption='[[6f64]], [[Resolution|resolution]] 2.49Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f64]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F64 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6F64 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f63|6f63]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYCP1, SCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6f64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f64 OCA], [http://pdbe.org/6f64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f64 RCSB], [http://www.ebi.ac.uk/pdbsum/6f64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f64 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SYCP1_HUMAN SYCP1_HUMAN]] Major component of the transverse filaments of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for normal assembly of the central element of the synaptonemal complexes. Required for normal centromere pairing during meiosis. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility.[UniProtKB:Q62209] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Meiotic chromosomes adopt unique structures in which linear arrays of chromatin loops are bound together in homologous chromosome pairs by a supramolecular protein assembly, the synaptonemal complex. This three-dimensional scaffold provides the essential structural framework for genetic exchange by crossing over and subsequent homolog segregation. The core architecture of the synaptonemal complex is provided by SYCP1. Here we report the structure and self-assembly mechanism of human SYCP1 through X-ray crystallographic and biophysical studies. SYCP1 has an obligate tetrameric structure in which an N-terminal four-helical bundle bifurcates into two elongated C-terminal dimeric coiled-coils. This building block assembles into a zipper-like lattice through two self-assembly sites. N-terminal sites undergo cooperative head-to-head assembly in the midline, while C-terminal sites interact back to back on the chromosome axis. Our work reveals the underlying molecular structure of the synaptonemal complex in which SYCP1 self-assembly generates a supramolecular lattice that mediates meiotic chromosome synapsis. | |||
Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly.,Dunce JM, Dunne OM, Ratcliff M, Millan C, Madgwick S, Uson I, Davies OR Nat Struct Mol Biol. 2018 Jun 18. pii: 10.1038/s41594-018-0078-9. doi:, 10.1038/s41594-018-0078-9. PMID:29915389<ref>PMID:29915389</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Davies, O | <div class="pdbe-citations 6f64" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Davies, O R]] | |||
[[Category: Dunce, J M]] | |||
[[Category: Millan, C]] | [[Category: Millan, C]] | ||
[[Category: Uson, I]] | [[Category: Uson, I]] | ||
[[Category: | [[Category: Chromosome structure]] | ||
[[Category: Coiled-coil]] | |||
[[Category: Meiosis]] | |||
[[Category: Self-assembly]] | |||
[[Category: Structural protein]] | |||
Latest revision as of 08:57, 22 April 2020
Crystal structure of the SYCP1 C-terminal back-to-back assemblyCrystal structure of the SYCP1 C-terminal back-to-back assembly
Structural highlights
Function[SYCP1_HUMAN] Major component of the transverse filaments of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for normal assembly of the central element of the synaptonemal complexes. Required for normal centromere pairing during meiosis. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility.[UniProtKB:Q62209] Publication Abstract from PubMedMeiotic chromosomes adopt unique structures in which linear arrays of chromatin loops are bound together in homologous chromosome pairs by a supramolecular protein assembly, the synaptonemal complex. This three-dimensional scaffold provides the essential structural framework for genetic exchange by crossing over and subsequent homolog segregation. The core architecture of the synaptonemal complex is provided by SYCP1. Here we report the structure and self-assembly mechanism of human SYCP1 through X-ray crystallographic and biophysical studies. SYCP1 has an obligate tetrameric structure in which an N-terminal four-helical bundle bifurcates into two elongated C-terminal dimeric coiled-coils. This building block assembles into a zipper-like lattice through two self-assembly sites. N-terminal sites undergo cooperative head-to-head assembly in the midline, while C-terminal sites interact back to back on the chromosome axis. Our work reveals the underlying molecular structure of the synaptonemal complex in which SYCP1 self-assembly generates a supramolecular lattice that mediates meiotic chromosome synapsis. Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly.,Dunce JM, Dunne OM, Ratcliff M, Millan C, Madgwick S, Uson I, Davies OR Nat Struct Mol Biol. 2018 Jun 18. pii: 10.1038/s41594-018-0078-9. doi:, 10.1038/s41594-018-0078-9. PMID:29915389[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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