5FJZ

Yeast delta-COP-I mu-homology domain complexed with Dsl1 WxWxV peptide

5FJZ の概要

• エントリーDOI: 10.2210/pdb5fjz/pdb
• 関連するPDBエントリー: 5FJW 5FJX 5FK0
• 分子名称: COATOMER SUBUNIT DELTA, PROTEIN TRANSPORT PROTEIN DSL1 (3 entities in total)
• 機能のキーワード: protein transport, cop-i, vesicle coat protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Cytoplasm : P43621 P43621; Endoplasmic reticulum membrane ; Peripheral membrane protein : P53847
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 123961.37

構造登録者

Suckling, R.J.,Evans, P.R.,Owen, D.J. (登録日: 2015-10-14, 公開日: 2015-11-11, 最終更新日: 2024-01-10)

主引用文献

Suckling, R.J.,Poon, P.P.,Travis, S.M.,Majoul, I.V.,Hughson, F.M.,Evans, P.R.,Duden, R.,Owen, D.J.
Structural Basis for the Binding of Tryptophan-Based Motifs by Delta-Cop.
Proc.Natl.Acad.Sci.USA, 112:14242-, 2015

PubMed Abstract: Coatomer consists of two subcomplexes: the membrane-targeting, ADP ribosylation factor 1 (Arf1):GTP-binding βγδζ-COP F-subcomplex, which is related to the adaptor protein (AP) clathrin adaptors, and the cargo-binding αβ'ε-COP B-subcomplex. We present the structure of the C-terminal μ-homology domain of the yeast δ-COP subunit in complex with the WxW motif from its binding partner, the endoplasmic reticulum-localized Dsl1 tether. The motif binds at a site distinct from that used by the homologous AP μ subunits to bind YxxΦ cargo motifs with its two tryptophan residues sitting in compatible pockets. We also show that the Saccharomyces cerevisiae Arf GTPase-activating protein (GAP) homolog Gcs1p uses a related WxxF motif at its extreme C terminus to bind to δ-COP at the same site in the same way. Mutations designed on the basis of the structure in conjunction with isothermal titration calorimetry confirm the mode of binding and show that mammalian δ-COP binds related tryptophan-based motifs such as that from ArfGAP1 in a similar manner. We conclude that δ-COP subunits bind Wxn(1-6)[WF] motifs within unstructured regions of proteins that influence the lifecycle of COPI-coated vesicles; this conclusion is supported by the observation that, in the context of a sensitizing domain deletion in Dsl1p, mutating the tryptophan-based motif-binding site in yeast causes defects in both growth and carboxypeptidase Y trafficking/processing.

PubMed: 26578768
DOI: 10.1073/PNAS.1506186112

実験手法

X-RAY DIFFRACTION (1.9 Å)