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1ROW

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

Summary for 1ROW
Entry DOI10.2210/pdb1row/pdb
Related1M1S
DescriptorMSP-domain protein like family member (2 entities in total)
Functional Keywordsbeta barrel, structural genomics, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, structural protein
Biological sourceCaenorhabditis elegans
Total number of polymer chains2
Total formula weight22044.97
Authors
Primary citationSchormann, N.,Symersky, J.,Luo, M.
Structure of sperm-specific protein SSP-19 from Caenorhabditis elegans.
Acta Crystallogr.,Sect.D, 60:1840-1845, 2004
Cited by
PubMed Abstract: 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.
PubMed: 15388931
DOI: 10.1107/S0907444904017846
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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