3obw

<table><tr><td colspan='2'>[[3obw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OBW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3OBW FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oby|3oby]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3obw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3obw OCA], [http://pdbe.org/3obw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3obw RCSB], [http://www.ebi.ac.uk/pdbsum/3obw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3obw ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PELO_SULSO PELO_SULSO]] May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity (By similarity).

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== Publication Abstract from PubMed ==

Dom34 from Saccharomyces cerevisiae is one of the key players in no-go mRNA decay, a surveillance pathway by which an abnormal mRNA stalled during translation is degraded by an endonucleolytic cleavage. Its homologs called Pelota are found in other species. We showed previously that S. cerevisiae Dom34 (domain 1) has an endoribonuclease activity, which suggests its direct catalytic role in no-go decay. Pelota from Thermoplasma acidophilum and Dom34 from S. cerevisiae have been structurally characterized, revealing a tripartite architecture with a significant difference in their overall conformations. To gain further insights into structural plasticity of the Pelota proteins, we have determined the crystal structures of two archaeal Pelotas from Archaeoglobus fulgidus and Sulfolobus solfataricus. Despite the structural similarity of their individual domains to those of T. acidophilum Pelota and S. cerevisiae Dom34, their overall conformations are distinct from those of T. acidophilum Pelota and S. cerevisiae Dom34. Different overall conformations are due to conformational flexibility of the two linker regions between domains 1 and 2 and between domains 2 and 3. The observed inter-domain structural plasticity of Pelota proteins suggests that large conformational changes are essential for their functions.

Crystal structures of two archaeal Pelotas reveal inter-domain structural plasticity.,Lee HH, Jang JY, Yoon HJ, Kim SJ, Suh SW Biochem Biophys Res Commun. 2010 Aug 1. PMID:20682285<ref>PMID:20682285</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3obw" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 35091]]

[[Category: Jang, J Y]]

[[Category: Kim, S J]]

[[Category: Lee, H H]]

[[Category: Suh, S W]]

[[Category: Yoon, H J]]

[[Category: Sm fold]]