3fht: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of human Dbp5 in complex with AMPPNP and RNA== | ==Crystal structure of human Dbp5 in complex with AMPPNP and RNA== | ||
<StructureSection load='3fht' size='340' side='right' caption='[[3fht]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3fht' size='340' side='right' caption='[[3fht]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| Line 6: | Line 7: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fhc|3fhc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fhc|3fhc]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX19B (Dbp5) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX19B (Dbp5) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<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=3fht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fht OCA], [http://pdbe.org/3fht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fht RCSB], [http://www.ebi.ac.uk/pdbsum/3fht PDBsum]</span></td></tr> | <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=3fht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fht OCA], [http://pdbe.org/3fht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fht RCSB], [http://www.ebi.ac.uk/pdbsum/3fht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fht ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 14: | Line 15: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fht_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fht_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:09, 5 December 2018
Crystal structure of human Dbp5 in complex with AMPPNP and RNACrystal structure of human Dbp5 in complex with AMPPNP and RNA
Structural highlights
Function[DD19B_HUMAN] ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe DEAD-box protein DBP5 is essential for mRNA export in both yeast and humans. It binds RNA and is concentrated and locally activated at the cytoplasmic side of the nuclear pore complex. We have determined the crystal structures of human DBP5 bound to RNA and AMPPNP, and bound to the cytoplasmic nucleoporin NUP214. The structures reveal that binding of DBP5 to nucleic acid and to NUP214 is mutually exclusive. Using in vitro assays, we demonstrate that NUP214 decreases both the RNA binding and ATPase activities of DBP5. The interactions are mediated by conserved residues, implying a conserved recognition mechanism. These results suggest a framework for the consecutive steps leading to the release of mRNA at the final stages of nuclear export. More generally, they provide a paradigm for how binding of regulators can specifically inhibit DEAD-box proteins. The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner.,von Moeller H, Basquin C, Conti E Nat Struct Mol Biol. 2009 Feb 15. PMID:19219046[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||||
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Conti, E
- Moeller, H von
- Atp-binding
- Can
- Dbp5
- Ddx19b
- Dead-box helicase
- Gle1
- Helicase
- Hydrolase
- Hydrolase-rna complex
- Membrane
- Mrna export
- Mrna transport
- Nuclear pore
- Nuclear pore complex
- Nucleocytoplasmic transport
- Nucleotide-binding
- Nucleus
- Nup159
- Nup214
- Phosphoprotein
- Protein transport
- Rna dependent atpase
- Rna-binding
- Translocation
- Transport