1YGT

Dynein Light Chain TcTex-1

Summary for 1YGT

• Entry DOI: 10.2210/pdb1ygt/pdb
• Descriptor: Cytoplasmic dynein light chain, SULFATE ION (3 entities in total)
• Functional Keywords: domain swapping, protein transport
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Cytoplasm, cytoskeleton (Probable): Q94524
• Total number of polymer chains: 1
• Total formula weight: 12587.08

Authors

Williams, J.C.,Xie, H.,Hendrickson, W.A. (deposition date: 2005-01-05, release date: 2005-02-15, Last modification date: 2024-02-14)

Primary citation

Williams, J.C.,Xie, H.,Hendrickson, W.A.
Crystal structure of dynein light chain TcTex-1.
J.Biol.Chem., 280:21981-21986, 2005

PubMed Abstract: TcTex-1, one of three dynein light chains of the dynein motor complex, has been implicated in targeting and binding cargoes to cytoplasmic dynein for retrograde or apical transport. Interactions between TcTex-1 and a diverse set of proteins such as the dynein intermediate chain, Fyn, DOC2, FIP1, the poliovirus receptor, CD155, and the rhodopsin cytoplasmic tail have been reported; yet, despite the broad range of targets, a consensus binding sequence remains uncertain. Consequently, we have solved the crystal structure of the full-length Drosophila homolog of TcTex-1 to 1.7 A resolution using MAD phasing to gain insight into its function and target specificity. The structure is homodimeric with a domain swapping of beta-strand 2 and has a fold similar to the dynein light chain, LC8. Based on structural alignment, the TcTex-1 and LC8 sequences show no identity, although the root mean square deviation between secondary structural elements is less than 1.6 A. Moreover, the N terminus, which is equivalent to beta-strand 1 in LC8, is splayed out and binds to a crystallographic dimer as an anti-parallel beta-strand at the same position as the neuronal nitric-oxide synthase peptide in the LC8 complex. Similarity to LC8 and comparison to the LC8-neuronal nitricoxide synthase complex suggest that TcTex-1 binds its targets in a similar manner as LC8 and provides insight to the lack of strict sequence identity among the targets for TcTex-1.

PubMed: 15701632
DOI: 10.1074/jbc.M414643200

Experimental method

X-RAY DIFFRACTION (1.7 Å)