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A novel RING finger in the C-terminal domain of the coatomer protein ?-COP.

ABSTRACT: The C-terminal domain of ?-COP, an essential subunit of the COPI coatomer complex, is composed of an all ?-helical region and a small ?-sheet domain. We show that this ?-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.

SUBMITTER: Kaur G

PROVIDER: S-EPMC4678705 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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A novel RING finger in the C-terminal domain of the coatomer protein α-COP.

Kaur Gurmeet G Subramanian Srikrishna S

Biology direct 20151214

The C-terminal domain of α-COP, an essential subunit of the COPI coatomer complex, is composed of an all α-helical region and a small β-sheet domain. We show that this β-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 memb ...[more]

PMID: 26666296

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