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| | ==Crystal Structure of Frog DGCR8 Dimerization Domain== | | ==Crystal Structure of Frog DGCR8 Dimerization Domain== |
| - | <StructureSection load='4e5r' size='340' side='right' caption='[[4e5r]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4e5r' size='340' side='right'caption='[[4e5r]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4e5r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E5R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4e5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E5R FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3le4|3le4]]</td></tr> | + | </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=4e5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e5r OCA], [https://pdbe.org/4e5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e5r RCSB], [https://www.ebi.ac.uk/pdbsum/4e5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e5r ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dgcr8, MGC78846 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</td></tr>
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| - | <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=4e5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e5r OCA], [http://pdbe.org/4e5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e5r RCSB], [http://www.ebi.ac.uk/pdbsum/4e5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e5r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/Q6IRB5_XENLA Q6IRB5_XENLA]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: African clawed frog]] | + | [[Category: Large Structures]] |
| - | [[Category: Barr, I]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Guo, F]] | + | [[Category: Barr I]] |
| - | [[Category: Laganowsky, A]] | + | [[Category: Guo F]] |
| - | [[Category: Scheidemantle, B D]] | + | [[Category: Laganowsky A]] |
| - | [[Category: Senturia, R]] | + | [[Category: Scheidemantle BD]] |
| - | [[Category: Dimerization]]
| + | [[Category: Senturia R]] |
| - | [[Category: Domain swapping]]
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| - | [[Category: Rna binding protein]]
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| - | [[Category: Ww motif]]
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| Structural highlights
Function
[Q6IRB5_XENLA]
Publication Abstract from PubMed
Human DiGeorge Critical Region 8 (DGCR8) is an essential microRNA (miRNA) processing factor that is activated via direct interaction with Fe(III) heme. In order for DGCR8 to bind heme, it must dimerize using a dimerization domain embedded within its heme-binding domain (HBD). We previously reported a crystal structure of the dimerization domain from human DGCR8, which demonstrated how dimerization results in the formation of a surface important for association with heme. Here, in an attempt to crystallize the HBD, we search for DGCR8 homologues and show that DGCR8 from Patiria miniata (bat star) also binds heme. The extinction coefficients (epsilon) of DGCR8-heme complexes are determined; these values are useful for biochemical analyses and allow us to estimate the heme occupancy of DGCR8 proteins. Additionally, we present the crystal structure of the Xenopus laevis dimerization domain. The structure is very similar to that of human DGCR8. Our results indicate that dimerization and heme binding are evolutionarily conserved properties of DGCR8 homologues not only in vertebrates, but also in at least some invertebrates.
Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8.,Senturia R, Laganowsky A, Barr I, Scheidemantle BD, Guo F PLoS One. 2012;7(7):e39688. Epub 2012 Jul 2. PMID:22768307[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Senturia R, Laganowsky A, Barr I, Scheidemantle BD, Guo F. Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8. PLoS One. 2012;7(7):e39688. Epub 2012 Jul 2. PMID:22768307 doi:http://dx.doi.org/10.1371/journal.pone.0039688
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