1yaf
From Proteopedia
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'''Structure of TenA from Bacillus subtilis''' | '''Structure of TenA from Bacillus subtilis''' | ||
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[[Category: Park, J H.]] | [[Category: Park, J H.]] | ||
[[Category: Toms, A V.]] | [[Category: Toms, A V.]] | ||
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Revision as of 13:04, 3 May 2008
Structure of TenA from Bacillus subtilis
Overview
Bacillus subtilis gene products TenA and TenI have been implicated in regulating the production of extracellular proteases, but their role in the regulation process remains unclear. The structural characterization of these proteins was undertaken to help provide insight into their function. We have determined the structure of TenA alone and in complex with 4-amino-2-methyl-5-hydroxymethylpyrimidine, and we demonstrate that TenA is a thiaminase II. The TenA structure suggests that the degradation of thiamin by TenA likely proceeds via the same addition-elimination mechanism described for thiaminase I. Three active-site residues, Asp44, Cys135, and Glu205, are likely involved in substrate binding and catalysis based on the enzyme/product complex structure and the conservation of these residues within TenA sequences. We have also determined the structure of TenI. Although TenI shows significant structural homology to thiamin phosphate synthase, it has no known enzymatic function. The structure suggests that TenI is unable to bind thiamin phosphate, largely resulting from the presence of leucine at position 119, while the corresponding residue in thiamin phosphate synthase is glycine.
About this Structure
1YAF is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II., Toms AV, Haas AL, Park JH, Begley TP, Ealick SE, Biochemistry. 2005 Feb 22;44(7):2319-29. PMID:15709744 Page seeded by OCA on Sat May 3 16:04:21 2008
