1LPL
Structural Genomics of Caenorhabditis elegans: CAP-Gly domain of F53F4.3
Summary for 1LPL
| Entry DOI | 10.2210/pdb1lpl/pdb |
| Descriptor | Hypothetical 25.4 kDa protein F53F4.3 in chromosome V (2 entities in total) |
| Functional Keywords | structural genomics, cap-gly domain, cytoskeleton, tubulin, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, unknown function |
| Biological source | Caenorhabditis elegans |
| Cellular location | Cytoplasm (By similarity): Q20728 |
| Total number of polymer chains | 1 |
| Total formula weight | 10358.67 |
| Authors | Li, S.,Finley, J.,Liu, Z.-J.,Qiu, S.H.,Luan, C.H.,Carson, M.,Tsao, J.,Johnson, D.,Lin, G.,Zhao, J.,Thomas, W.,Nagy, L.A.,Sha, B.,DeLucas, L.J.,Wang, B.-C.,Luo, M.,Southeast Collaboratory for Structural Genomics (SECSG) (deposition date: 2002-05-08, release date: 2002-05-22, Last modification date: 2024-02-14) |
| Primary citation | Li, S.,Finley, J.,Liu, Z.-J.,Qiu, S.H.,Luan, C.H.,Carson, M.,Tsao, J.,Johnson, D.,Lin, G.,Zhao, J.,Thomas, W.,Nagy, L.A.,Sha, B.,DeLucas, L.J.,Wang, B.-C.,Luo, M. Crystal Structure of the Cytoskeleton-associated Protein Glycine-rich (CAP-Gly) Domain J.Biol.Chem., 277:48596-48601, 2002 Cited by PubMed Abstract: Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three beta-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove. PubMed: 12221106DOI: 10.1074/jbc.M208512200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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