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Fig. 1. TbLC1 has sequence and structural homology to CrLC1. (A) Schematic diagram of the Chlamydomonas outer arm dynein complex [adapted from King (King, 2003) with permission]. It is composed of three heavy chains (HC), each associated with at least one light chain (LC). HCs have three regions, a globular head motor domain, a microtubule-binding stalk and a neck domain that contributes to correct cargo binding. (B) Sequence alignment between TbLC1 and LC1 homologues (accession numbers listed in Materials and Methods). There is strong conservation, particularly in the LRR region (underlined residues are 40.5% identical, 94.6% similar). Key residues are conserved including those predicted to bind the 
HC (#), p45 (*) and two C-terminal basic residues (x) thought to contact the ATP-hydrolyzing site in the motor domain. Yellow and blue highlighted amino acids are identical between all and most organisms, respectively. Green highlighted amino acids represent conservative substitutions. (C) Space filling model of CrLC1 compared with TbLC1. The TbLC1 structure was predicted by sequence comparison to CrLC1 and modeling on the confirmed CrLC1 structure (Wu et al., 2000) as described in the Materials and Methods. CrLC1 residues predicted to bind the HC (green) as well as the basic residues in the C-terminus (blue) are conserved in the T. brucei protein. Red, 
-helices; yellow, 
-sheets.
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