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Fusion surface structure, function, and dynamics of gamete fusogen HAP2.
- Source :
-
ELife [Elife] 2018 Oct 03; Vol. 7. Date of Electronic Publication: 2018 Oct 03. - Publication Year :
- 2018
-
Abstract
- 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.<br />Competing Interests: JF, XD, JP, JZ, CL, RI, JE, WS, TS No competing interests declared<br /> (© 2018, Feng et al.)
- Subjects :
- Algal Proteins chemistry
Algal Proteins genetics
Amino Acid Sequence
Chlamydomonas reinhardtii genetics
Models, Molecular
Mutation
Protein Domains
Protein Multimerization
Protein Structure, Secondary
Sequence Homology, Amino Acid
Algal Proteins metabolism
Chlamydomonas reinhardtii metabolism
Membrane Fusion
Spores metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2050-084X
- Volume :
- 7
- Database :
- MEDLINE
- Journal :
- ELife
- Publication Type :
- Academic Journal
- Accession number :
- 30281023
- Full Text :
- https://doi.org/10.7554/eLife.39772