1g25
From Proteopedia
(New page: 200px<br /> <applet load="1g25" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g25" /> '''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN...) |
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| - | [[Image:1g25.gif|left|200px]]<br /> | + | [[Image:1g25.gif|left|200px]]<br /><applet load="1g25" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1g25" size=" | + | |
caption="1g25" /> | caption="1g25" /> | ||
'''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN TFIIH MAT1 SUBUNIT'''<br /> | '''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN TFIIH MAT1 SUBUNIT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human MAT1 protein belongs to the cyclin-dependent kinase-activating | + | The human MAT1 protein belongs to the cyclin-dependent kinase-activating kinase complex, which is functionally associated to the transcription/DNA repair factor TFIIH. The N-terminal region of MAT1 consists of a C3HC4 RING finger, which contributes to optimal TFIIH transcriptional activities. We report here the solution structure of the human MAT1 RING finger domain (Met(1)-Asp(65)) as determined by (1)H NMR spectroscopy. The MAT1 RING finger domain presents the expected betaalphabetabeta topology with two interleaved zinc-binding sites conserved among the RING family. However, the presence of an additional helical segment in the N-terminal part of the domain and a conserved hydrophobic central beta strand are the defining features of this new structure and more generally of the MAT1 RING finger subfamily. Comparison of electrostatic surfaces of RING finger structures shows that the RING finger domain of MAT1 presents a remarkable positively charged surface. The functional implications of these MAT1 RING finger features are discussed. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1G25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G25 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Busso, D.]] | [[Category: Busso, D.]] | ||
| - | [[Category: Egly, J | + | [[Category: Egly, J M.]] |
[[Category: Gervais, V.]] | [[Category: Gervais, V.]] | ||
[[Category: Kieffer, B.]] | [[Category: Kieffer, B.]] | ||
[[Category: Poterszman, A.]] | [[Category: Poterszman, A.]] | ||
| - | [[Category: Thierry, J | + | [[Category: Thierry, J C.]] |
[[Category: Wasielewski, E.]] | [[Category: Wasielewski, E.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: ring finger (c3hc4)]] | [[Category: ring finger (c3hc4)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:13 2008'' |
Revision as of 10:45, 21 February 2008
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SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN TFIIH MAT1 SUBUNIT
Contents |
Overview
The human MAT1 protein belongs to the cyclin-dependent kinase-activating kinase complex, which is functionally associated to the transcription/DNA repair factor TFIIH. The N-terminal region of MAT1 consists of a C3HC4 RING finger, which contributes to optimal TFIIH transcriptional activities. We report here the solution structure of the human MAT1 RING finger domain (Met(1)-Asp(65)) as determined by (1)H NMR spectroscopy. The MAT1 RING finger domain presents the expected betaalphabetabeta topology with two interleaved zinc-binding sites conserved among the RING family. However, the presence of an additional helical segment in the N-terminal part of the domain and a conserved hydrophobic central beta strand are the defining features of this new structure and more generally of the MAT1 RING finger subfamily. Comparison of electrostatic surfaces of RING finger structures shows that the RING finger domain of MAT1 presents a remarkable positively charged surface. The functional implications of these MAT1 RING finger features are discussed.
Disease
Known diseases associated with this structure: Hypermethioninemia, persistent, autosomal dominant, due to methionine adenosyltransferase I/III deficiency OMIM:[250850], Methionine adenosyltransferase deficiency, autosomal recessive OMIM:[250850]
About this Structure
1G25 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of the N-terminal domain of the human TFIIH MAT1 subunit: new insights into the RING finger family., Gervais V, Busso D, Wasielewski E, Poterszman A, Egly JM, Thierry JC, Kieffer B, J Biol Chem. 2001 Mar 9;276(10):7457-64. Epub 2000 Oct 30. PMID:11056162
Page seeded by OCA on Thu Feb 21 12:45:13 2008
