ISDA: 1MP9

Deposition Date 2002-09-12

Release Date 2003-11-04

Last Version Date 2024-03-13

Entry Detail

PDB ID:

1MP9

Keywords:

DNA BINDING PROTEIN

Title:

TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius

Biological Source:

Source Organism(s):

Sulfolobus acidocaldarius (Taxon ID: 2285)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.00 Å

R-Value Free:

0.25

R-Value Work:

0.20

R-Value Observed:

0.20

Space Group:

P 21 21 2

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:TATA-binding protein
Gene (Uniprot):tbp
Chain IDs:A, B
Chain Length:198
Number of Molecules:2
Biological Source:Sulfolobus acidocaldarius

UniProt ID:Q9UWN7 Pfam ID:PF00352

Primary Citation

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.Show

Structure 12 157 168 (2004)

PMID: 14725775 DOI: 10.1016/j.str.2003.12.003

Abstact

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.

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Primary Citation of related structures

Abstact

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