1mp9: Difference between revisions

Revision as of 00:40, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mp9.png

Template:STRUCTURE 1mp9

TBP from a mesothermophilic archaeon, Sulfolobus acidocaldariusTBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius

Template:ABSTRACT PUBMED 14725775

About this StructureAbout this Structure

1MP9 is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.

ReferenceReference

Origins of protein stability revealed by comparing crystal structures of TATA binding proteins., Koike H, Kawashima-Ohya Y, Yamasaki T, Clowney L, Katsuya Y, Suzuki M, Structure. 2004 Jan;12(1):157-68. PMID:14725775

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius'''
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-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14725775}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_14725775}}
 ==About this Structure==
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