1yaf
From Proteopedia
(New page: 200px<br /><applet load="1yaf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yaf, resolution 2.60Å" /> '''Structure of TenA fr...) |
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| - | [[Image:1yaf.gif|left|200px]]<br /><applet load="1yaf" size=" | + | [[Image:1yaf.gif|left|200px]]<br /><applet load="1yaf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yaf, resolution 2.60Å" /> | caption="1yaf, resolution 2.60Å" /> | ||
'''Structure of TenA from Bacillus subtilis'''<br /> | '''Structure of TenA from Bacillus subtilis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacillus subtilis gene products TenA and TenI have been implicated in | + | 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== | ==About this Structure== | ||
| - | 1YAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1YAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YAF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Begley, T | + | [[Category: Begley, T P.]] |
| - | [[Category: Ealick, S | + | [[Category: Ealick, S E.]] |
| - | [[Category: Haas, A | + | [[Category: Haas, A L.]] |
| - | [[Category: Park, J | + | [[Category: Park, J H.]] |
| - | [[Category: Toms, A | + | [[Category: Toms, A V.]] |
[[Category: thiaminase]] | [[Category: thiaminase]] | ||
[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:17 2008'' |
Revision as of 14:03, 21 February 2008
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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
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