6e18
From Proteopedia
(Difference between revisions)
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<StructureSection load='6e18' size='340' side='right' caption='[[6e18]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='6e18' size='340' side='right' caption='[[6e18]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6e18]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E18 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e18]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E18 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HAP2, GCS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e18 OCA], [http://pdbe.org/6e18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e18 RCSB], [http://www.ebi.ac.uk/pdbsum/6e18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e18 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e18 OCA], [http://pdbe.org/6e18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e18 RCSB], [http://www.ebi.ac.uk/pdbsum/6e18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e18 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/HAP2_CHLRE HAP2_CHLRE]] During fertilization, required on male (minus) gametes for their fusion with female (plus) gametes (PubMed:18367645, PubMed:20335357, PubMed:25655701, PubMed:28235200). Required for membrane fusion, but not for the initial adhesion between gametes (PubMed:18367645, PubMed:25655701, PubMed:28235200). Inserts (via its extracellular domain) into lipid membranes (in vitro) (PubMed:28235200). Probably initiates the fusion of gamete cell membranes by inserting its extracellular domain into the cell membrane of a female gamete (PubMed:28235200).<ref>PMID:18367645</ref> <ref>PMID:20335357</ref> <ref>PMID:25655701</ref> <ref>PMID:28235200</ref> | [[http://www.uniprot.org/uniprot/HAP2_CHLRE HAP2_CHLRE]] During fertilization, required on male (minus) gametes for their fusion with female (plus) gametes (PubMed:18367645, PubMed:20335357, PubMed:25655701, PubMed:28235200). Required for membrane fusion, but not for the initial adhesion between gametes (PubMed:18367645, PubMed:25655701, PubMed:28235200). Inserts (via its extracellular domain) into lipid membranes (in vitro) (PubMed:28235200). Probably initiates the fusion of gamete cell membranes by inserting its extracellular domain into the cell membrane of a female gamete (PubMed:28235200).<ref>PMID:18367645</ref> <ref>PMID:20335357</ref> <ref>PMID:25655701</ref> <ref>PMID:28235200</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The cellular fusion protein HAP2, which is structurally homologous to viral class II fusion proteins, drives gamete fusion across several eukaryotic kingdoms. Gamete fusion is a highly controlled process in eukaryotes, and is allowed only between same species gametes. In spite of a conserved architecture, HAP2 displays several species-specific functional regions that were not resolved in the available X-ray structure of the green alga Chlamydomonas reinhardtii HAP2 ectodomain. Here we present an X-ray structure resolving these regions, showing a target membrane interaction surface made by three amphipathic helices in a horseshoe-shaped arrangement. HAP2 from green algae also features additional species-specific motifs inserted in regions that in viral class II proteins are critical for the fusogenic conformational change. Such insertions include a cystine ladder-like module evocative of EGF-like motifs responsible for extracellular protein-protein interactions in animals, and a mucin-like region. These features suggest potential HAP2 interaction sites involved in gamete fusion control. | ||
| + | |||
| + | Species-Specific Functional Regions of the Green Alga Gamete Fusion Protein HAP2 Revealed by Structural Studies.,Baquero E, Fedry J, Legrand P, Krey T, Rey FA Structure. 2018 Oct 19. pii: S0969-2126(18)30361-7. doi:, 10.1016/j.str.2018.09.014. PMID:30416037<ref>PMID:30416037</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6e18" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Chlre]] | ||
[[Category: Baquero, E]] | [[Category: Baquero, E]] | ||
[[Category: Legrand, P]] | [[Category: Legrand, P]] | ||
Revision as of 20:59, 2 December 2018
Crystal structure of Chlamydomonas reinhardtii HAP2 ectodomain provides structural insights of functional loops in green algae.
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