1g25
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(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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Revision as of 14:53, 12 November 2007
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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 ZN 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
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