1Y4O

Solution structure of a mouse cytoplasmic Roadblock/LC7 dynein light chain

Summary for 1Y4O

• Entry DOI: 10.2210/pdb1y4o/pdb
• NMR Information: BMRB: 6396
• Descriptor: Dynein light chain 2A, cytoplasmic (1 entity in total)
• Functional Keywords: structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, dynein light chain, contractile protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm, cytoskeleton: P62627
• Total number of polymer chains: 2
• Total formula weight: 23999.32

Authors

Song, J.,Tyler, R.C.,Lee, M.S.,Tyler, E.M.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-12-01, release date: 2005-01-18, Last modification date: 2024-05-22)

Primary citation

Song, J.,Tyler, R.C.,Lee, M.S.,Tyler, E.M.,Markley, J.L.
Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex.
J.Mol.Biol., 354:1043-1051, 2005

PubMed Abstract: Roadblock/LC7 is a member of a class of dynein light chains involved in regulating the function of the dynein complex. We have determined the three-dimensional structure of isoform 1 of the mouse Roadblock/LC7 cytoplasmic dynein light chain (robl1_mouse) by NMR spectroscopy. In contrast to a previously reported NMR structure of the human homolog with 96% sequence identity (PDB 1TGQ), which showed the protein as a monomer, our results indicate clearly that robl1 exists as a symmetric homodimer. The two beta3-strands pair with each other and form a continuous ten-stranded beta-sheet. The 25-residue alpha2-helix from one subunit packs antiparallel to that of the other subunit on the face of the beta-sheet. Zipper-like hydrophobic contacts between the two helices serve to stabilize the dimer. Through an NMR titration experiment, we localized the site on robl1_mouse that interacts with the 40 residue peptide spanning residues 243 through 282 of IC74-1_rat. These results provide physical evidence for a symmetrical interaction between dimeric robl1 and the two molecules of IC74-1 in the dynein complex.

PubMed: 16289575
DOI: 10.1016/j.jmb.2005.10.017

Experimental method

SOLUTION NMR