1oqj
From Proteopedia
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|PDB= 1oqj |SIZE=350|CAPTION= <scene name='initialview01'>1oqj</scene>, resolution 1.55Å | |PDB= 1oqj |SIZE=350|CAPTION= <scene name='initialview01'>1oqj</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= GMEB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= GMEB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1h5p|1H5P]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqj OCA], [http://www.ebi.ac.uk/pdbsum/1oqj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oqj RCSB]</span> | ||
}} | }} | ||
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[[Category: Scheffzek, K.]] | [[Category: Scheffzek, K.]] | ||
[[Category: Surdo, P L.]] | [[Category: Surdo, P L.]] | ||
| - | [[Category: ZN]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
[[Category: kdwk motif]] | [[Category: kdwk motif]] | ||
| Line 32: | Line 34: | ||
[[Category: zinc-binding motif]] | [[Category: zinc-binding motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:54 2008'' |
Revision as of 19:48, 30 March 2008
| |||||||
| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GMEB1 (Homo sapiens) | ||||||
| Related: | 1H5P
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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