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1mp9
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp9 OCA], [http://www.ebi.ac.uk/pdbsum/1mp9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mp9 RCSB]</span> | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:18 2008'' |
Revision as of 19:19, 30 March 2008
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| , resolution 2.000Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius
Overview
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.
About this Structure
1MP9 is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.
Reference
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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