2gv5
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crystal structure of Sfi1p/Cdc31p complex
OverviewOverview
Centrins are calmodulin-like proteins present in centrosomes and yeast, spindle pole bodies (SPBs) and have essential functions in their, duplication. The Saccharomyces cerevisiae centrin, Cdc31p, binds Sfi1p on, multiple conserved repeats; both proteins localize to the SPB half-bridge, where the new SPB is assembled. The crystal structures of Sfi1p-centrin, complexes containing several repeats show Sfi1p as an alpha helix with, centrins wrapped around each repeat and similar centrin-centrin contacts, between each repeat. Electron microscopy (EM) shadowing of an, Sfi1p-centrin complex with 15 Sfi1 repeats and 15 centrins bound showed, filaments 60 nm long, compatible with all the Sfi1 repeats as a continuous, alpha helix. Immuno-EM localization of the Sfi1p N and C termini showed, Sfi1p-centrin filaments spanning the length of the half-bridge with the, Sfi1p N terminus at the SPB. This suggests a model for SPB duplication, where the half-bridge doubles in length by association of the Sfi1p C, termini, thereby providing a new Sfi1p N terminus to initiate SPB, assembly.
About this StructureAbout this Structure
2GV5 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication., Li S, Sandercock AM, Conduit P, Robinson CV, Williams RL, Kilmartin JV, J Cell Biol. 2006 Jun 19;173(6):867-77. PMID:16785321
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