Steve Ealick's Research Group
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Steve Ealick's Research Group |
TenI from Bacillus subtilis
PDB file:
Description:
B. subtilis TenI is a 22,783 Da protein that is not essential for growth in thiamin containing media. In Bacillis subtilis, TenA and TenI are part of the thiazole biosynthetic operon (TenA-TenI-ThiO-ThiS-ThiG-ThiF-ThiD). The function of TenI is unknown, however it attenuates the stimulation of the production of degradative enzymes by TenA at the transcriptional level.
| The TenI momoner has (βα)8 barrel fold. The monomer consists of a mainly hydrophobic core formed by residues from the β-strands that point into the interior of the barrel. |
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| The TenI crystal structure consists of two (βα)8 barrel dimers, with the barrel axes for each dimer oriented approximately parallel to each other. Two monomers are related by one NCS twofold axis and the other two are related by a second NCS twofold axis. Within each dimer, the primary interactions between monomers are hydrophobic. |
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| The TenI sulfate binding site is at the N-terminus of α8a in each monomer. Each sulfate ion has hydrogen binding interactions with several residues as well as with three water molecules. |
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Reference:
Toms AV, Haas AL, Park J-H, Begley TP and Ealick SE. Structural Characterization of the Regulatory Proteins TenA and TenI from Bacillus subtilis and the identification of TenA as a Thiaminase II. Biochemistry 44:2319-2329 (2005).
