1row

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Structure of SSP-19, an MSP-domain protein like family member in Caenorhabditis elegans

Overview

Structural data are reported for SSP-19, a sperm-specific protein (SSP), family member from Caenorhabditis elegans. The SSP family [also known as, the major sperm protein-like (MSP-like) family] contains proteins with, only 107-109 amino acids, compared with 127 amino acids in the major sperm, protein (MSP) family. MSP, the most abundant protein in nematode sperm, forms a dynamic actin-like cytoskeleton that provides the framework for, the nematode sperm motility. In vivo, MSP dimers polymerize to form, filaments that are constructed from two helical strands, which assemble, into larger macromolecular structures. Little is known about the SSP, family and a similar function is inferred from sequence and structural, homology [Pfam (Protein Families Database of Alignments and HMMs) and SCOP, (Structural Classification of Proteins) classification]. Despite the, overall structural homology, the monomer-monomer interactions in SSP-19, are strikingly different from the interactions in the two MSP canonic, domains described previously.

About this Structure

1ROW is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Structure of sperm-specific protein SSP-19 from Caenorhabditis elegans., Schormann N, Symersky J, Luo M, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1840-5. Epub 2004, Sep 23. PMID:15388931

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