1IMJ
CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)
Summary for 1IMJ
| Entry DOI | 10.2210/pdb1imj/pdb |
| Descriptor | CCG1-INTERACTING FACTOR B, SULFATE ION (3 entities in total) |
| Functional Keywords | alpha/beta hydrolase, ccg1 interactor, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q96IU4 |
| Total number of polymer chains | 1 |
| Total formula weight | 22461.65 |
| Authors | Padmanabhan, B.,Kuzuhara, T.,Horikoshi, M. (deposition date: 2001-05-11, release date: 2002-05-11, Last modification date: 2024-03-13) |
| Primary citation | 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 Cited by 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: 14672934DOI: 10.1074/jbc.M312165200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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