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3OBY

Crystal structure of Archaeoglobus fulgidus Pelota reveals inter-domain structural plasticity

Summary for 3OBY
Entry DOI10.2210/pdb3oby/pdb
Related3OBW
DescriptorProtein pelota homolog (2 entities in total)
Functional Keywordssm fold, hydrolase
Biological sourceArchaeoglobus fulgidus
Cellular locationCytoplasm (Potential): O29421
Total number of polymer chains2
Total formula weight80546.11
Authors
Lee, H.H.,Jang, J.Y.,Yoon, H.-J.,Kim, S.J.,Suh, S.W. (deposition date: 2010-08-09, release date: 2010-09-01, Last modification date: 2024-03-20)
Primary citationLee, H.H.,Jang, J.Y.,Yoon, H.-J.,Kim, S.J.,Suh, S.W.
Crystal structures of two archaeal Pelotas reveal inter-domain structural plasticity
Biochem.Biophys.Res.Commun., 399:600-606, 2010
Cited by
PubMed Abstract: 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.
PubMed: 20682285
DOI: 10.1016/j.bbrc.2010.07.121
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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数据于2025-07-23公开中

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