Journal
BIOLOGY DIRECT
Volume 10, Issue -, Pages -Publisher
BMC
DOI: 10.1186/s13062-015-0099-9
Keywords
Cellular transport; Coat protein; Coated vesicles; Tethering complex; Zinc finger
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Funding
- XII Five-year plan network project GENESIS [BSC0121]
- Council of Scientific and Industrial Research (CSIR) - Institute of Microbial Technology, Chandigarh, India [OLP_0072]
- Shyama Prasad Mukherjee Fellowship of CSIR, India
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The C-terminal domain of alpha-COP, an essential subunit of the COPI coatomer complex, is composed of an all alpha- helical region and a small beta-sheet domain. We show that this beta-sheet domain is a Really Interesting New Gene (RING)-like treble clef zinc finger. The zinc-binding residues are substituted by other aminoacids in many homologs including the structurally-characterized proteins from Saccharomyces cerevisiae and Bos taurus. This RING-like domain is possibly related to those of other vesicle membrane-associated complexes, such as CORVET, HOPS and SEA, and likely mediates interactions with Dsl1p and assist in coat oligomerization.
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