1oqj
From Proteopedia
(New page: 200px<br /> <applet load="1oqj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oqj, resolution 1.55Å" /> '''Crystal structure o...) |
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| - | [[Image:1oqj.gif|left|200px]]<br /> | + | [[Image:1oqj.gif|left|200px]]<br /><applet load="1oqj" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oqj" size=" | + | |
caption="1oqj, resolution 1.55Å" /> | caption="1oqj, resolution 1.55Å" /> | ||
'''Crystal structure of the SAND domain from glucocorticoid modulatory element binding protein-1 (GMEB1)'''<br /> | '''Crystal structure of the SAND domain from glucocorticoid modulatory element binding protein-1 (GMEB1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The glucocorticoid-modulatory element-binding proteins, GMEB1 and GMEB2, are ubiquitous, multifunctional DNA-binding proteins with important roles | + | The glucocorticoid-modulatory element-binding proteins, GMEB1 and GMEB2, are ubiquitous, multifunctional DNA-binding proteins with important roles in the modulation of transcription upon steroid hormone activation. The GMEB proteins have intrinsic transactivation ability, but also control the glucocorticoid response via direct binding to the glucocorticoid receptor. They are also mandatory host proteins for Parvovirus replication. Here we present the 1.55 A resolution crystal structure of a central portion of GMEB1, encompassing its SAND domain, which shares 80% sequence identity with the GMEB2 SAND domain. We demonstrate that this domain, also present in numerous proteins implicated in chromatin-associated transcriptional regulation, is necessary and sufficient to bind the glucocorticoid-modulatory element (GME) DNA target. We use nuclear magnetic resonance (NMR) and binding studies to map the DNA recognition surface to an alpha-helical region exposing the conserved KDWK motif. Using site-directed mutagenesis, key residues for DNA binding are identified. In contrast to the previously determined NMR structure of the Sp100b SAND domain, we find that the GMEB1 SAND domain also comprises a zinc-binding motif. Although the zinc ion is not necessary for DNA binding, it is found to determine the C-terminal conformation of the GMEB1 SAND domain. We also show that homologous zinc-binding motifs exist in a subset of SAND domain proteins and probe the roles of this novel motif. |
==About this Structure== | ==About this Structure== | ||
| - | 1OQJ 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:// | + | 1OQJ 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=1OQJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bottomley, M | + | [[Category: Bottomley, M J.]] |
[[Category: Sattler, M.]] | [[Category: Sattler, M.]] | ||
[[Category: Scheffzek, K.]] | [[Category: Scheffzek, K.]] | ||
| - | [[Category: Surdo, P | + | [[Category: Surdo, P L.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
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[[Category: zinc-binding motif]] | [[Category: zinc-binding motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:28 2008'' |
Revision as of 12:20, 21 February 2008
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Crystal structure of the SAND domain from glucocorticoid modulatory element binding protein-1 (GMEB1)
Overview
The glucocorticoid-modulatory element-binding proteins, GMEB1 and GMEB2, are ubiquitous, multifunctional DNA-binding proteins with important roles in the modulation of transcription upon steroid hormone activation. The GMEB proteins have intrinsic transactivation ability, but also control the glucocorticoid response via direct binding to the glucocorticoid receptor. They are also mandatory host proteins for Parvovirus replication. Here we present the 1.55 A resolution crystal structure of a central portion of GMEB1, encompassing its SAND domain, which shares 80% sequence identity with the GMEB2 SAND domain. We demonstrate that this domain, also present in numerous proteins implicated in chromatin-associated transcriptional regulation, is necessary and sufficient to bind the glucocorticoid-modulatory element (GME) DNA target. We use nuclear magnetic resonance (NMR) and binding studies to map the DNA recognition surface to an alpha-helical region exposing the conserved KDWK motif. Using site-directed mutagenesis, key residues for DNA binding are identified. In contrast to the previously determined NMR structure of the Sp100b SAND domain, we find that the GMEB1 SAND domain also comprises a zinc-binding motif. Although the zinc ion is not necessary for DNA binding, it is found to determine the C-terminal conformation of the GMEB1 SAND domain. We also show that homologous zinc-binding motifs exist in a subset of SAND domain proteins and probe the roles of this novel motif.
About this Structure
1OQJ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure and nuclear magnetic resonance analyses of the SAND domain from glucocorticoid modulatory element binding protein-1 reveals deoxyribonucleic acid and zinc binding regions., Surdo PL, Bottomley MJ, Sattler M, Scheffzek K, Mol Endocrinol. 2003 Jul;17(7):1283-95. Epub 2003 Apr 17. PMID:12702733
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