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Fusion surface structure, function, and dynamics of gamete fusogen HAP2

Juan Feng, Xianchi Dong, Jennifer F. Pinello, Jun Zhang, Chafen Lu, Roxana E. Iacob, John R Engen, Wiliam J. Snell, Timothy A. Springer
doi: https://doi.org/10.1101/324194
Juan Feng
1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Childrens Hospital Boston, 3 Blackfan Circle, Boston MA 02115
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Xianchi Dong
1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Childrens Hospital Boston, 3 Blackfan Circle, Boston MA 02115
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Jennifer F. Pinello
2Department of Cell Biology and Molecular Genetics, U. Maryland, 4066 Campus Drive, College Park MD 20742
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Jun Zhang
2Department of Cell Biology and Molecular Genetics, U. Maryland, 4066 Campus Drive, College Park MD 20742
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Chafen Lu
1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Childrens Hospital Boston, 3 Blackfan Circle, Boston MA 02115
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Roxana E. Iacob
3Department of Chemistry & Chemical Biology, Northeastern University, Boston, MA 02115
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John R Engen
3Department of Chemistry & Chemical Biology, Northeastern University, Boston, MA 02115
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Wiliam J. Snell
2Department of Cell Biology and Molecular Genetics, U. Maryland, 4066 Campus Drive, College Park MD 20742
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  • For correspondence: Lu@crystal.harvard.edu Springer@crystal.harvard.edu
Timothy A. Springer
1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Childrens Hospital Boston, 3 Blackfan Circle, Boston MA 02115
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  • For correspondence: Lu@crystal.harvard.edu Springer@crystal.harvard.edu
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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 loop 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 long fusion loop, 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.

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Posted May 16, 2018.
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Fusion surface structure, function, and dynamics of gamete fusogen HAP2
Juan Feng, Xianchi Dong, Jennifer F. Pinello, Jun Zhang, Chafen Lu, Roxana E. Iacob, John R Engen, Wiliam J. Snell, Timothy A. Springer
bioRxiv 324194; doi: https://doi.org/10.1101/324194
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Fusion surface structure, function, and dynamics of gamete fusogen HAP2
Juan Feng, Xianchi Dong, Jennifer F. Pinello, Jun Zhang, Chafen Lu, Roxana E. Iacob, John R Engen, Wiliam J. Snell, Timothy A. Springer
bioRxiv 324194; doi: https://doi.org/10.1101/324194

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