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| | ==Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit== | | ==Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit== |
| - | <StructureSection load='1z60' size='340' side='right' caption='[[1z60]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1z60' size='340' side='right'caption='[[1z60]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1z60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e53 1e53]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z60 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1z60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e53 1e53]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z60 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z60 OCA], [http://pdbe.org/1z60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z60 RCSB], [http://www.ebi.ac.uk/pdbsum/1z60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z60 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1z60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z60 OCA], [https://pdbe.org/1z60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z60 RCSB], [https://www.ebi.ac.uk/pdbsum/1z60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z60 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TF2H2_HUMAN TF2H2_HUMAN]] Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. The N-terminus interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter. | + | [https://www.uniprot.org/uniprot/TF2H2_HUMAN TF2H2_HUMAN] Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. The N-terminus interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Boelens, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Dominguez, C]] | + | [[Category: Boelens R]] |
| - | [[Category: Fribourg, S]] | + | [[Category: Dominguez C]] |
| - | [[Category: Kellenberger, E]] | + | [[Category: Fribourg S]] |
| - | [[Category: Kieffer, B]] | + | [[Category: Kellenberger E]] |
| - | [[Category: Moras, D]] | + | [[Category: Kieffer B]] |
| - | [[Category: Poterszman, A]] | + | [[Category: Moras D]] |
| - | [[Category: Wasielewski, E]] | + | [[Category: Poterszman A]] |
| - | [[Category: Basic transcription factor]]
| + | [[Category: Wasielewski E]] |
| - | [[Category: Ring finger]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Zinc binding protein]]
| + | |
| Structural highlights
Function
TF2H2_HUMAN Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. The N-terminus interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter.
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 PubMed
The human general transcription factor TFIIH is involved in both transcription and DNA nucleotide excision repair. Among the 10 subunits of the complex, p44 subunit plays a crucial role in both mechanisms. Its N-terminal domain interacts with the XPD helicase, whereas its C-terminal domain is involved specifically in the promoter escape activity. By mutating an exposed and non-conserved cysteine residue into a serine, we produced a soluble mutant of p44-(321-395) suitable for solution structure determination. The domain adopts a C4C4 RING domain structure with sequential organization of beta-strands that is related to canonical RING domains by a circular permutation of the beta-sheet elements. Analysis of the molecular surface and mutagenesis experiments suggests that the binding of p44-(321-395) to TFIIH p34 subunit is not mediated by electrostatic interactions and, thus, differs from previously reported interaction mechanisms involving RING domains.
Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions.,Kellenberger E, Dominguez C, Fribourg S, Wasielewski E, Moras D, Poterszman A, Boelens R, Kieffer B J Biol Chem. 2005 May 27;280(21):20785-92. Epub 2005 Mar 24. PMID:15790571[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kellenberger E, Dominguez C, Fribourg S, Wasielewski E, Moras D, Poterszman A, Boelens R, Kieffer B. Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions. J Biol Chem. 2005 May 27;280(21):20785-92. Epub 2005 Mar 24. PMID:15790571 doi:10.1074/jbc.M412999200
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