6dbs
From Proteopedia
(Difference between revisions)
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<StructureSection load='6dbs' size='340' side='right' caption='[[6dbs]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='6dbs' size='340' side='right' caption='[[6dbs]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6dbs]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DBS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DBS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dbs]] is a 3 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=6DBS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DBS FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=BMA:BETA-D-MANNOSE'>BMA</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=6dbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dbs OCA], [http://pdbe.org/6dbs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dbs RCSB], [http://www.ebi.ac.uk/pdbsum/6dbs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dbs 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=6dbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dbs OCA], [http://pdbe.org/6dbs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dbs RCSB], [http://www.ebi.ac.uk/pdbsum/6dbs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dbs 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 == | ||
+ | HAP2 is a class II gamete fusogen in many eukaryotic kingdoms. A crystal structure of Chlamydomonas HAP2 shows a trimeric fusion state. Domains D1, D2.1 and D2.2 line the 3-fold axis; D3 and a stem pack against the outer surface. Surprisingly, hydrogen-deuterium exchange shows that surfaces of D1, D2.2 and D3 closest to the 3-fold axis are more dynamic than exposed surfaces. Three fusion helices in the fusion loops of each monomer expose hydrophobic residues at the trimer apex that are splayed from the 3-fold axis, leaving a solvent-filled cavity between the fusion loops in each monomer. At the base of the two fusion loops, Arg185 docks in a carbonyl cage. Comparisons to other structures, dynamics, and the greater effect on Chlamydomonas gamete fusion of mutation of axis-proximal than axis-distal fusion helices suggest that the apical portion of each monomer could tilt toward the 3-fold axis with merger of the fusion helices into a common fusion surface. | ||
+ | |||
+ | Fusion surface structure, function, and dynamics of gamete fusogen HAP2.,Feng J, Dong X, Pinello J, Zhang J, Lu C, Iacob RE, Engen JR, Snell WJ, Springer TA Elife. 2018 Oct 3;7. pii: 39772. doi: 10.7554/eLife.39772. PMID:30281023<ref>PMID:30281023</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6dbs" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Chlre]] | ||
[[Category: Dong, X]] | [[Category: Dong, X]] | ||
[[Category: Feng, J]] | [[Category: Feng, J]] |
Revision as of 08:35, 17 October 2018
Fusion surface structure, function, and dynamics of gamete fusogen HAP2
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