1ds9

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ds9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds9 OCA], [http://www.ebi.ac.uk/pdbsum/1ds9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ds9 RCSB]</span>
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[[Category: leucine-rich repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:47:42 2008''

Revision as of 16:47, 30 March 2008


PDB ID 1ds9

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1


Overview

Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the gamma heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six beta-beta-alpha motifs. This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a hydrophobic surface within the repeat region that is proposed to interact with the dynein heavy chain. The position of the C-terminal domain on LC1 and the unexpected structural similarity between LC1 and U2A' from the human spliceosome suggest that this domain interacts with the dynein motor domain.

About this Structure

1DS9 is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

Reference

Solution structure of a dynein motor domain associated light chain., Wu H, Maciejewski MW, Marintchev A, Benashski SE, Mullen GP, King SM, Nat Struct Biol. 2000 Jul;7(7):575-9. PMID:10876244

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