Document Detail

Origins of protein stability revealed by comparing crystal structures of TATA binding proteins.
MedLine Citation:
PMID:  14725775     Owner:  NLM     Status:  MEDLINE    
The crystal structure of TATA binding protein (TBP) from a mesothermophilic archaeon, Sulfolobus acidocaldarius, has been determined at a resolution of 2.0 A with an R factor of 20.9%. By comparing this structure with the structures of TBPs from a hyperthermophilic archaeon and mesophilic eukaryotes, as well as by comparing amino acid sequences of TBPs from archaea, covering a wide range of optimum growth temperatures, two significant determinants of the stability of TBP have been identified: increasing the interior hydrophobicity by interaction between three residues, Val, Leu, and Ile, with further differentiation of the surface, and increasing its hydrophilicity and raising the cost of unfolding. These findings suggest directions along which the stability of TBP can be engineered.
Hideaki Koike; Yoshie Kawashima-Ohya; Tomoko Yamasaki; Lester Clowney; Yoshio Katsuya; Masashi Suzuki
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Structure (London, England : 1993)     Volume:  12     ISSN:  0969-2126     ISO Abbreviation:  Structure     Publication Date:  2004 Jan 
Date Detail:
Created Date:  2004-01-16     Completed Date:  2004-08-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  101087697     Medline TA:  Structure     Country:  United States    
Other Details:
Languages:  eng     Pagination:  157-68     Citation Subset:  IM    
National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Center 6-10, Higashi 1-1-1, Tsukuba 305-8566, Japan.
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MeSH Terms
Amino Acid Sequence
Archaea / genetics
Molecular Sequence Data
Molecular Structure
Sulfolobus acidocaldarius / chemistry*,  genetics
TATA-Box Binding Protein / chemistry*
Reg. No./Substance:
0/TATA-Box Binding Protein

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