1ROW
Structure of SSP-19, an MSP-domain protein like family member in Caenorhabditis elegans
Summary for 1ROW
| Entry DOI | 10.2210/pdb1row/pdb |
| Related | 1M1S |
| Descriptor | MSP-domain protein like family member (2 entities in total) |
| Functional Keywords | beta barrel, structural genomics, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, structural protein |
| Biological source | Caenorhabditis elegans |
| Total number of polymer chains | 2 |
| Total formula weight | 22044.97 |
| Authors | Schormann, N.,Symersky, J.,Carson, M.,Luo, M.,Lin, G.,Li, S.,Qiu, S.,Arabashi, A.,Bunzel, B.,Luo, D.,Nagy, L.,Gray, R.,Luan, C.-H.,Zhang, J.,Lu, S.,DeLucas, L.,Southeast Collaboratory for Structural Genomics (SECSG) (deposition date: 2003-12-02, release date: 2003-12-23, Last modification date: 2023-08-23) |
| Primary citation | Schormann, 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: 15388931DOI: 10.1107/S0907444904017846 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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