1XDX

Solution Structure of the Tctex1 Light Chain From Chlamydomonas Inner Dynein Arm I1

Summary for 1XDX

• Entry DOI: 10.2210/pdb1xdx/pdb
• NMR Information: BMRB: 4929
• Descriptor: Tctex1 Light Chain protein (1 entity in total)
• Functional Keywords: chlamydomonas flagella, tctex1 dimer, nmr solution structure, contractile protein
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 2
• Total formula weight: 25360.85

Authors

Wu, H.,Maciejewski, M.W.,Takebe, S.,King, S.M. (deposition date: 2004-09-08, release date: 2005-03-01, Last modification date: 2024-05-22)

Primary citation

Wu, H.,Maciejewski, M.W.,Takebe, S.,King, S.M.
Solution Structure of the Tctex1 Dimer Reveals a Mechanism for Dynein-Cargo Interactions
Structure, 13:213-223, 2005

PubMed Abstract: Tctex1 is a light chain found in both cytoplasmic and flagellar dyneins and is involved in many fundamental cellular activities, including rhodopsin transport within photoreceptors, and may function in the non-Mendelian transmission of t haplotypes in mice. Here, we present the NMR solution structure for the Tctex1 dimer from Chlamydomonas axonemal inner dynein arm I1. Structural comparisons reveal a strong similarity with the LC8 dynein light chain dimer, including formation of a strand-switched beta sheet interface. Analysis of the Tctex1 structure enables the dynein intermediate chain binding site to be identified and suggests a mechanism by which cargo proteins might be attached to this microtubule motor complex. Comparison with the alternate dynein light chain rp3 reveals how the specificity of dynein-cargo interactions mediated by these dynein components is achieved. In addition, this structure provides insight into the consequences of the mutations found in the t haplotype forms of this protein.

PubMed: 15698565
DOI: 10.1016/j.str.2004.11.013

Experimental method

SOLUTION NMR