7KYS

Crystal structure of human BCCIP beta (Native2)

7KYS の概要

• エントリーDOI: 10.2210/pdb7kys/pdb
• 分子名称: BRCA2 and CDKN1A-interacting protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: brca2, eif6, cancer suppressor, ribosome biogenesis, gnat, gcn5-related acetyltransferase, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 88651.48

構造登録者

Choi, W.S.,Liu, B.,Shen, Z.,Yang, W. (登録日: 2020-12-08, 公開日: 2021-06-09, 最終更新日: 2023-10-18)

主引用文献

Choi, W.S.,Liu, B.,Shen, Z.,Yang, W.
Structure of human BCCIP and implications for binding and modification of partner proteins.
Protein Sci., 30:693-699, 2021

PubMed Abstract: BCCIP was isolated based on its interactions with tumor suppressors BRCA2 and p21. Knockdown or knockout of BCCIP causes embryonic lethality in mice. BCCIP deficient cells exhibit impaired cell proliferation and chromosome instability. BCCIP also plays a key role in biogenesis of ribosome 60S subunits. BCCIP is conserved from yeast to humans, but it has no discernible sequence similarity to proteins of known structures. Here we report two crystal structures of an N-terminal truncated human BCCIPβ, consisting of residues 61-314. Structurally BCCIP is similar to GCN5-related acetyltransferases (GNATs) but contains different sequence motifs. Moreover, both acetyl-CoA and substrate-binding grooves are altered in BCCIP. A large 19-residue flap over the putative CoA binding site adopts either an open or closed conformation in BCCIP. The substrate binding groove is significantly reduced in size and is positively charged despite the acidic isoelectric point of BCCIP. BCCIP has potential binding sites for partner proteins and may have enzymatic activity.

PubMed: 33452718
DOI: 10.1002/pro.4026

実験手法

X-RAY DIFFRACTION (2.2 Å)