2.6 A resolution crystal structure of helices of the motile major sperm protein (MSP) of Caenorhabditis elegans

Journal of Molecular Biology
Anne M E BakerMurray Stewart


The amoeboid locomotion of nematode sperm is mediated by the assembly dynamics of the major sperm protein (MSP). MSP forms fibrous networks based on a hierarchy of macromolecular assemblies: helical subfilaments are built from MSP dimers; filaments are formed from two subfilaments coiling round one another; and filaments themselves supercoil to produce bundles. To provide a structural context for understanding the role of these macromolecular assemblies in cell locomotion, we have determined the 2.6 A resolution structure of crystals of Caenorhabditis elegans MSP that are constructed from helices of MSP chains that are analogous to the subfilaments from which filaments are constructed. Comparison with the crystal structures of dimers and helical assemblies of Ascaris suum MSP has identified five conserved interaction interfaces that suggest how subfilaments interact in filaments and how filaments can form bundles. The interfaces frequently involve the loop containing residues 78-85, which is divergent between MSP homologues, and the loop containing residues 98-103, which is highly conserved.


Mar 1, 1991·Acta Crystallographica. Section A, Foundations of Crystallography·T A JonesM Kjeldgaard
Jul 12, 1996·Journal of Molecular Biology·A HaafM Stewart
May 1, 1996·Journal of Structural Biology·T L BullockM Stewart
Oct 25, 1996·Journal of Molecular Biology·T L BullockM Stewart
Mar 21, 1998·Nature Structural Biology·T L BullockM Stewart
Oct 3, 1998·Acta Crystallographica. Section D, Biological Crystallography·A T BrüngerG L Warren
Nov 4, 2000·International Review of Cytology·J E ItalianoT M Roberts
Sep 1, 1994·Acta Crystallographica. Section D, Biological Crystallography·UNKNOWN Collaborative Computational Project, Number 4

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