4kbg: Difference between revisions
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==almost closed conformation of the helicase core of the RNA helicase Hera== | |||
=== | <StructureSection load='4kbg' size='340' side='right' caption='[[4kbg]], [[Resolution|resolution]] 2.54Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4kbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KBG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ear|3ear]], [[3eas|3eas]], [[3eaq|3eaq]], [[4kbf|4kbf]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C1895 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=4kbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kbg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kbg RCSB], [http://www.ebi.ac.uk/pdbsum/4kbg PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DEAD-box helicases catalyze the ATP-dependent destabilization of RNA duplexes. Hera is a DEAD-box helicase from Thermus thermophilus that consists of a helicase core, followed by a C-terminal extension comprising a dimerization domain and an RNA-binding domain. The combined structural information on individual Hera domains provides a molecular model of the Hera dimer. The modular architecture with flexible connections between individual domains affords different relative orientations of the RBD relative to the Hera helicase core, and of the two helicase cores within the dimer. Presumably, domain movements are intimately linked to RNA binding, to the interplay of the RBD and the helicase core, and to RNA unwinding, and may impact on the functional cooperation of the two helicase cores in RNA unwinding. The in vivo function of Hera is unknown. The Hera RBD recognizes two distinct elements in the RNA substrate, a single-stranded and a structured region. The helicase core then unwinds an adjacent RNA duplex in an ATP-dependent reaction. Overall, this mode of action is reminiscent of DEAD-box proteins that act as general RNA chaperones. This review summarizes the current knowledge on Hera structure and function, and discusses a possible role of Hera in the Thermus thermophilus cold-shock response. | |||
Rearranging RNA structures at 75 degrees C? towards the molecular mechanism and physiological function of the Thermus thermophilus DEAD-box helicase hera.,Klostermeier D Biopolymers. 2013 Jun 13. doi: 10.1002/bip.22316. PMID:23765433<ref>PMID:23765433</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Thet2]] | [[Category: Thet2]] | ||
[[Category: Klostermeier, D | [[Category: Klostermeier, D]] | ||
[[Category: Rudolph, M G | [[Category: Rudolph, M G]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Dead box rna helicase]] | [[Category: Dead box rna helicase]] | ||