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1imj

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|PDB= 1imj |SIZE=350|CAPTION= <scene name='initialview01'>1imj</scene>, resolution 2.20&Aring;
|PDB= 1imj |SIZE=350|CAPTION= <scene name='initialview01'>1imj</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1imj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1imj OCA], [http://www.ebi.ac.uk/pdbsum/1imj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1imj RCSB]</span>
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[[Category: Kuzuhara, T.]]
[[Category: Kuzuhara, T.]]
[[Category: Padmanabhan, B.]]
[[Category: Padmanabhan, B.]]
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[[Category: SO4]]
 
[[Category: alpha/beta hydrolase]]
[[Category: alpha/beta hydrolase]]
[[Category: ccg1 interactor]]
[[Category: ccg1 interactor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:21:56 2008''

Revision as of 18:21, 30 March 2008

Image:1imj.jpg


PDB ID 1imj

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1IMJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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