1IMJ

CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)

1IMJ の概要

• エントリーDOI: 10.2210/pdb1imj/pdb
• 分子名称: CCG1-INTERACTING FACTOR B, SULFATE ION (3 entities in total)
• 機能のキーワード: alpha/beta hydrolase, ccg1 interactor, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q96IU4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22461.65

構造登録者

Padmanabhan, B.,Kuzuhara, T.,Horikoshi, M. (登録日: 2001-05-11, 公開日: 2002-05-11, 最終更新日: 2024-03-13)

主引用文献

Padmanabhan, B.,Kuzuhara, T.,Adachi, N.,Horikoshi, M.
The crystal structure of CCG1/TAF(II)250-interacting factor B (CIB)
J.Biol.Chem., 279:9615-9624, 2004

PubMed Abstract: The general transcription initiation factor TFIID and its interactors play critical roles in regulating the transcription from both naked and chromatin DNA. We have isolated a novel TFIID interactor that we denoted as CCG1/TAF(II)250-interacting factor B (CIB). We show here that CIB activates transcription. To further understand the function of this protein, we determined its crystal structure at 2.2-Angstroms resolution. The tertiary structure of CIB reveals an alpha/beta-hydrolase fold that resembles structures in the prokaryotic alpha/beta-hydrolase family proteins. It is not similar in structure or primary sequence to any eukaryotic transcription or chromatin factors that have been reported to date. CIB possesses a conserved catalytic triad that is found in other alpha/beta-hydrolases, and our in vitro studies confirmed that it bears hydrolase activity. However, CIB differs from other alpha/beta-hydrolases in that it lacks a binding site excursion, which facilitates the substrate selectivity of the other alpha/beta-hydrolases. Further functional characterization of CIB based on its tertiary structure and through biochemical studies may provide novel insights into the mechanisms that regulate eukaryotic transcription.

PubMed: 14672934
DOI: 10.1074/jbc.M312165200

実験手法

X-RAY DIFFRACTION (2.2 Å)