Title : The crystal structure of CCG1\/TAF(II)250-interacting factor B (CIB) - Padmanabhan_2004_J.Biol.Chem_279_9615 |
Author(s) : Padmanabhan B , Kuzuhara T , Adachi N , Horikoshi M |
Ref : Journal of Biological Chemistry , 279 :9615 , 2004 |
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. |
PubMedSearch : Padmanabhan_2004_J.Biol.Chem_279_9615 |
PubMedID: 14672934 |
Gene_locus related to this paper: human-CIB |
Gene_locus | human-CIB |
Family | CIB-CCG1-interacting-factor-B |
Structure | 1IMJ |
Padmanabhan B, Kuzuhara T, Adachi N, Horikoshi M (2004)
The crystal structure of CCG1\/TAF(II)250-interacting factor B (CIB)
Journal of Biological Chemistry
279 :9615
Padmanabhan B, Kuzuhara T, Adachi N, Horikoshi M (2004)
Journal of Biological Chemistry
279 :9615