This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. WD repeat proteins are very common in eukaryotes (1% of all yeast proteins) and mediate many different signaling pathways by functioning as a protein-binding module. Prior structural studies are very limited. The transducin b subunit model reveals that it folds into a seven-bladed propeller which result from the presence of 7 WD repeats. We have recently elucidated the structure of Bub3p from S. cerevisiae, a protein thought to contain 4 WD repeats and found that it, too, folds into a seven bladed propeller. To determine whether the seven-bladed fold is general (implying that many WD repeats have yet to be found in sequence searches) or if these proteins are capable of containing a variable number of repeats, we have crystallized three proteins with an 'irregular' number of repeats which have been identified by the sequence. These structures will allow us to more confidently predict the fold of others in this ubiquitous family of proteins. They will also provide a framework for future studies to determine whether WD proteins bind their partner proteins in a similar manner.
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