2HF6

Solution structure of human zeta-COP

2HF6 の概要

• エントリーDOI: 10.2210/pdb2hf6/pdb
• 分子名称: Coatomer subunit zeta-1 (1 entity in total)
• 機能のキーワード: cop i, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): P61923
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17049.58

構造登録者

Yu, W.,Jin, C.,Xia, B. (登録日: 2006-06-23, 公開日: 2007-06-12, 最終更新日: 2024-05-01)

主引用文献

Yu, W.,Lin, J.,Jin, C.,Xia, B.
Solution structure of human zeta-COP: direct evidences for structural similarity between COP I and clathrin-adaptor coats
J.Mol.Biol., 386:903-912, 2009

PubMed Abstract: COP-I-coated vesicles are protein and lipid carriers that mediate intra-Golgi transport and transport from the cis-Golgi complex to the endoplasmic reticulum in cells. The coatomer of the vesicles coat is comprised of seven subunits: alpha-COP, epsilon-COP, beta'-COP, beta-COP, gamma-COP, delta-COP, and zeta-COP. Here we report the solution structure of a truncated form (residues 1-149; zeta-COP149) of human zeta-COP (total 177 residues). It is the first three-dimensional structure of a "core" subunit of the COP I F-subcomplex. The structure of zeta-COP149 mainly consists of a disordered N-terminal tail, a five-stranded antiparallel beta-sheet, a two-stranded antiparallel beta-sheet, and five alpha-helices. The global folding of zeta-COP149 is very similar to the crystal structures of AP1-sigma1 and AP2-sigma2, directly demonstrating the structural similarity between the "core" subunits of the COP I F-subcomplex and adaptor protein complexes. Through structural comparison and mutagenesis study, we have also demonstrated that the heterodimers of zeta-COP149 and gamma-COP have packing interfaces and relative subunit orientations similar to those of AP2-sigma2 and AP2-alpha heterodimers. These results provide direct evidence supporting the previous proposal that the COP I F-subcomplex and adaptor protein complexes have similar tertiary and quaternary structures.

PubMed: 19167404
DOI: 10.1016/j.jmb.2008.12.083

実験手法

SOLUTION NMR