ISDA: 1IUK

Deposition Date 2002-03-05

Release Date 2003-07-15

Last Version Date 2023-10-25

Entry Detail

PDB ID:

1IUK

Keywords:

STRUCTURAL GENOMICS, UNKNOWN FUNCTION

Title:

The structure of native ID.343 from Thermus thermophilus

Biological Source:

Source Organism(s):

Thermus thermophilus (Taxon ID: 274)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.70 Å

R-Value Free:

0.28

R-Value Work:

0.22

R-Value Observed:

0.23

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:hypothetical protein TT1466
Chain IDs:A
Chain Length:140
Number of Molecules:1
Biological Source:Thermus thermophilus

UniProt ID:Q8GHJ5 Pfam ID:PF13380

Primary Citation

Structure of a conserved CoA-binding protein synthesized by a cell-free system.

Wada, T, Shirouzu, M, Terada, T, Ishizuka, Y, Matsuda, T, Kigawa, T, Kuramitsu, S, Park, S.Y, Tame, J.R, Yokoyama, S.Show

Acta Crystallogr. D Biol. Crystallogr. 59 1213 1218 (2003)

PMID: 12832765 DOI: 10.1107/S0907444903010515

Abstact

TT1466 is a hypothetical protein from the extremely thermophilic bacterium Thermus thermophilus HB8 and is highly conserved in bacteria and archaea. The selenomethionyl protein was synthesized by a cell-free system and the crystal structure was determined at 2.0 A by MAD phasing. A native crystal was used for structure refinement to 1.7 A. The structure is highly homologous to that of the CoA-binding domain of the succinyl-CoA synthetase from Escherichia coli, despite the protein having only 14% sequence identity to this domain. An isothermal titration calorimetry experiment was performed to investigate whether TT1466 binds CoA and revealed high-affinity CoA binding of TT1466.

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Primary Citation of related structures

Abstact

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