1rtw
From Proteopedia
(New page: 200px<br /><applet load="1rtw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rtw, resolution 2.35Å" /> '''X-ray Structure of P...) |
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| - | [[Image:1rtw.gif|left|200px]]<br /><applet load="1rtw" size=" | + | [[Image:1rtw.gif|left|200px]]<br /><applet load="1rtw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rtw, resolution 2.35Å" /> | caption="1rtw, resolution 2.35Å" /> | ||
'''X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34'''<br /> | '''X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34'''<br /> | ||
==Overview== | ==Overview== | ||
| - | TenA (transcriptional enhancer A) has been proposed to function as a | + | TenA (transcriptional enhancer A) has been proposed to function as a transcriptional regulator based on observed changes in gene-expression patterns when overexpressed in Bacillus subtilis. However, studies of the distribution of proteins involved in thiamine biosynthesis in different fully sequenced genomes have suggested that TenA may be an enzyme involved in thiamine biosynthesis, with a function related to that of the ThiC protein. The crystal structure of PF1337, the TenA homolog from Pyrococcus furiosus, is presented here. The protomer comprises a bundle of alpha-helices with a similar tertiary structure and topology to that of human heme oxygenase-1, even though there is no significant sequence homology. A solvent-sequestered cavity lined by phylogenetically conserved residues is found at the core of this bundle in PF1337 and this cavity is observed to contain electron density for 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate, the product of the ThiC enzyme. In contrast, the modestly acidic surface of PF1337 shows minimal levels of sequence conservation and a dearth of the basic residues that are typically involved in DNA binding in transcription factors. Without significant conservation of its surface properties, TenA is unlikely to mediate functionally important protein-protein or protein-DNA interactions. Therefore, the crystal structure of PF1337 supports the hypothesis that TenA homologs have an indirect effect in altering gene-expression patterns and function instead as enzymes involved in thiamine metabolism. |
==About this Structure== | ==About this Structure== | ||
| - | 1RTW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_dsm_3638 Pyrococcus furiosus dsm 3638] with PO4 and MP5 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RTW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_dsm_3638 Pyrococcus furiosus dsm 3638] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MP5:'>MP5</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pyrococcus furiosus dsm 3638]] | [[Category: Pyrococcus furiosus dsm 3638]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Acton, T | + | [[Category: Acton, T B.]] |
[[Category: Benach, J.]] | [[Category: Benach, J.]] | ||
| - | [[Category: Edstrom, W | + | [[Category: Edstrom, W C.]] |
| - | [[Category: Hunt, J | + | [[Category: Hunt, J F.]] |
[[Category: Lee, I.]] | [[Category: Lee, I.]] | ||
| - | [[Category: Montelione, G | + | [[Category: Montelione, G T.]] |
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: Rong, X.]] | [[Category: Rong, X.]] | ||
[[Category: MP5]] | [[Category: MP5]] | ||
| Line 33: | Line 33: | ||
[[Category: thiamin]] | [[Category: thiamin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:33 2008'' |
Revision as of 12:54, 21 February 2008
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X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34
Overview
TenA (transcriptional enhancer A) has been proposed to function as a transcriptional regulator based on observed changes in gene-expression patterns when overexpressed in Bacillus subtilis. However, studies of the distribution of proteins involved in thiamine biosynthesis in different fully sequenced genomes have suggested that TenA may be an enzyme involved in thiamine biosynthesis, with a function related to that of the ThiC protein. The crystal structure of PF1337, the TenA homolog from Pyrococcus furiosus, is presented here. The protomer comprises a bundle of alpha-helices with a similar tertiary structure and topology to that of human heme oxygenase-1, even though there is no significant sequence homology. A solvent-sequestered cavity lined by phylogenetically conserved residues is found at the core of this bundle in PF1337 and this cavity is observed to contain electron density for 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate, the product of the ThiC enzyme. In contrast, the modestly acidic surface of PF1337 shows minimal levels of sequence conservation and a dearth of the basic residues that are typically involved in DNA binding in transcription factors. Without significant conservation of its surface properties, TenA is unlikely to mediate functionally important protein-protein or protein-DNA interactions. Therefore, the crystal structure of PF1337 supports the hypothesis that TenA homologs have an indirect effect in altering gene-expression patterns and function instead as enzymes involved in thiamine metabolism.
About this Structure
1RTW is a Single protein structure of sequence from Pyrococcus furiosus dsm 3638 with and as ligands. Full crystallographic information is available from OCA.
Reference
The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism., Benach J, Edstrom WC, Lee I, Das K, Cooper B, Xiao R, Liu J, Rost B, Acton TB, Montelione GT, Hunt JF, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):589-98. Epub 2005, Apr 20. PMID:15858269
Page seeded by OCA on Thu Feb 21 14:54:33 2008
Categories: Pyrococcus furiosus dsm 3638 | Single protein | Acton, T B. | Benach, J. | Edstrom, W C. | Hunt, J F. | Lee, I. | Montelione, G T. | NESG, Northeast Structural Genomics Consortium. | Rong, X. | MP5 | PO4 | Crystal structure | Nesg | Northeast structural genomics consortium | Pf1337 | Protein structure initiative | Psi | Structural genomics | Tena | Thiamin
