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1imj

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Current revision (13:24, 13 March 2024) (edit) (undo)
 
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<StructureSection load='1imj' size='340' side='right'caption='[[1imj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1imj' size='340' side='right'caption='[[1imj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1imj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IMJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1imj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IMJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1imj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1imj OCA], [https://pdbe.org/1imj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1imj RCSB], [https://www.ebi.ac.uk/pdbsum/1imj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1imj ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1imj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1imj OCA], [https://pdbe.org/1imj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1imj RCSB], [https://www.ebi.ac.uk/pdbsum/1imj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1imj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ABHEB_HUMAN ABHEB_HUMAN]] Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription.<ref>PMID:14672934</ref>
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[https://www.uniprot.org/uniprot/ABHEB_HUMAN ABHEB_HUMAN] Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription.<ref>PMID:14672934</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1imj ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1imj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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<ref>PMID:14672934</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1imj" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Horikoshi, M]]
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[[Category: Horikoshi M]]
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[[Category: Kuzuhara, T]]
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[[Category: Kuzuhara T]]
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[[Category: Padmanabhan, B]]
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[[Category: Padmanabhan B]]
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[[Category: Alpha/beta hydrolase]]
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[[Category: Ccg1 interactor]]
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[[Category: Hydrolase]]
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Current revision

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

PDB ID 1imj

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