Document Detail


Influence of cation-pi interactions to the structural stability of prokaryotic and eukaryotic translation elongation factors.
MedLine Citation:
PMID:  19653064     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have investigated the role of cation-pi interactions on translation elongation factors. In our investigation, an average of four significant cation-pi interactions were found, that is, an average of one cation-pi interaction per 44 residues in the ten elongation factors were observed. The analysis on the influence of short (< + or - 4), medium (> + or - 4 to < + or - 20) and long (>20) range contacts showed that cation-pi interactions are mainly formed by medium and long-range contacts. Arg-Tyr pair was found largest in number but energetic contribution of Arg-Trp pair was found most. Preferred secondary structural conformation analysis of the residues involved in cation-pi interaction indicates that the cationic Arg prefers to be in helix and Lys having equal probability for helix and strand, whereas the aromatic Phe and Trp were found mostly in helix while Tyr in strand regions. The cation-pi interaction residues involved in these proteins were found highly conserved with 48.86% residues having conservation score of > or = 6. Analysis of secondary structure preference of the energetically significant cation-pi residues in different solvent accessible range indicates that most of the pi residues are found buried or partially buried whereas cationic residues were found mostly at the protein surface. The results presented in this study will be useful for structural stability studies in translation elongation factors.
Authors:
Anand Anbarasu; Vibhu Ranjan Prasad; Shankha Sathpathy; Rao Sethumadhavan
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Publication Detail:
Type:  Journal Article     Date:  2009-08-05
Journal Detail:
Title:  Protoplasma     Volume:  238     ISSN:  1615-6102     ISO Abbreviation:  Protoplasma     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-11-12     Completed Date:  2010-03-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9806853     Medline TA:  Protoplasma     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  11-20     Citation Subset:  IM    
Affiliation:
School of Biotechnology, Chemical Engineering and Biomedical Engineering, Vellore Institute of Technology, Vellore, Tamil Nadu 632014, India. vibhuranjanprasad2006@vit.ac.in
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / chemistry*
Bacterial Proteins / chemistry
Cations / chemistry*
Humans
Peptide Elongation Factors / chemistry*
RNA-Binding Proteins / chemistry
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Bacterial Proteins; 0/Cations; 0/Peptide Elongation Factors; 0/RNA-Binding Proteins
Comments/Corrections
Erratum In:
Protoplasma. 2009 Dec;238(1-4):21
Note: Anbarasu, Anand [added]; Sethumadhavan, Rao [added]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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