1rtw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rtw.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rtw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rtw| PDB=1rtw | SCENE= }}
{{STRUCTURE_1rtw| PDB=1rtw | SCENE= }}
-
'''X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15858269}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15858269 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15858269}}
==About this Structure==
==About this Structure==
Line 39: Line 43:
[[Category: Tena]]
[[Category: Tena]]
[[Category: Thiamin]]
[[Category: Thiamin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:54:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:07:42 2008''

Revision as of 12:07, 28 July 2008

Image:1rtw.png

Template:STRUCTURE 1rtw

X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34

Template:ABSTRACT PUBMED 15858269

About this Structure

1RTW is a Single protein structure of sequence from Pyrococcus furiosus dsm 3638. 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 Mon Jul 28 15:07:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rtw"
Personal tools