1imj | pdb_00001imj
CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)
Structural highlights
Function[ABHEB_HUMAN] Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The crystal structure of CCG1/TAF(II)250-interacting factor B (CIB).,Padmanabhan B, Kuzuhara T, Adachi N, Horikoshi M J Biol Chem. 2004 Mar 5;279(10):9615-24. Epub 2003 Dec 11. PMID:14672934[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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