1lj9

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(New page: 200px<br /><applet load="1lj9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lj9, resolution 1.60&Aring;" /> '''The crystal structur...)
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[[Image:1lj9.gif|left|200px]]<br /><applet load="1lj9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lj9, resolution 1.60&Aring;" />
caption="1lj9, resolution 1.60&Aring;" />
'''The crystal structure of the transcriptional regulator SlyA'''<br />
'''The crystal structure of the transcriptional regulator SlyA'''<br />
==Overview==
==Overview==
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The crystal structure of a SlyA transcriptional regulator at 1.6 A, resolution is presented, and structural relationships between members of, the MarR/SlyA family are discussed. The SlyA family, which includes SlyA, Rap, Hor, and RovA proteins, is widely distributed in bacterial and, archaeal genomes. Current evidence suggests that SlyA-like factors act as, repressors, activators, and modulators of gene transcription. These, proteins have been shown to up-regulate the expression of molecular, chaperones, acid-resistance proteins, and cytolysin, and down-regulate, several biosynthetic enzymes. The structure of SlyA from Enterococcus, faecalis, determined as a part of an ongoing structural genomics, initiative (www.mcsg.anl.gov), revealed the same winged helix DNA-binding, motif that was recently found in the MarR repressor from Escherichia coli, and the MexR repressor from Pseudomonas aeruginosa, a sequence homologue, of MarR. Phylogenetic analysis of the MarR/SlyA family suggests that Sly, is placed between the SlyA and MarR subfamilies and shows significant, sequence similarity to members of both subfamilies.
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The crystal structure of a SlyA transcriptional regulator at 1.6 A resolution is presented, and structural relationships between members of the MarR/SlyA family are discussed. The SlyA family, which includes SlyA, Rap, Hor, and RovA proteins, is widely distributed in bacterial and archaeal genomes. Current evidence suggests that SlyA-like factors act as repressors, activators, and modulators of gene transcription. These proteins have been shown to up-regulate the expression of molecular chaperones, acid-resistance proteins, and cytolysin, and down-regulate several biosynthetic enzymes. The structure of SlyA from Enterococcus faecalis, determined as a part of an ongoing structural genomics initiative (www.mcsg.anl.gov), revealed the same winged helix DNA-binding motif that was recently found in the MarR repressor from Escherichia coli and the MexR repressor from Pseudomonas aeruginosa, a sequence homologue of MarR. Phylogenetic analysis of the MarR/SlyA family suggests that Sly is placed between the SlyA and MarR subfamilies and shows significant sequence similarity to members of both subfamilies.
==About this Structure==
==About this Structure==
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1LJ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LJ9 OCA].
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1LJ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJ9 OCA].
==Reference==
==Reference==
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[[Category: Gornicki, P.]]
[[Category: Gornicki, P.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
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[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
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[[Category: MCSG, Midwest Center for Structural Genomics.]]
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[[Category: Wu, R.Y.]]
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[[Category: Wu, R Y.]]
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[[Category: Zhang, R.G.]]
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[[Category: Zhang, R G.]]
[[Category: hth dna binding protein]]
[[Category: hth dna binding protein]]
[[Category: mcsg]]
[[Category: mcsg]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:01:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:30 2008''

Revision as of 11:45, 21 February 2008


1lj9, resolution 1.60Å

Drag the structure with the mouse to rotate

The crystal structure of the transcriptional regulator SlyA

Overview

The crystal structure of a SlyA transcriptional regulator at 1.6 A resolution is presented, and structural relationships between members of the MarR/SlyA family are discussed. The SlyA family, which includes SlyA, Rap, Hor, and RovA proteins, is widely distributed in bacterial and archaeal genomes. Current evidence suggests that SlyA-like factors act as repressors, activators, and modulators of gene transcription. These proteins have been shown to up-regulate the expression of molecular chaperones, acid-resistance proteins, and cytolysin, and down-regulate several biosynthetic enzymes. The structure of SlyA from Enterococcus faecalis, determined as a part of an ongoing structural genomics initiative (www.mcsg.anl.gov), revealed the same winged helix DNA-binding motif that was recently found in the MarR repressor from Escherichia coli and the MexR repressor from Pseudomonas aeruginosa, a sequence homologue of MarR. Phylogenetic analysis of the MarR/SlyA family suggests that Sly is placed between the SlyA and MarR subfamilies and shows significant sequence similarity to members of both subfamilies.

About this Structure

1LJ9 is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.

Reference

Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor., Wu RY, Zhang RG, Zagnitko O, Dementieva I, Maltzev N, Watson JD, Laskowski R, Gornicki P, Joachimiak A, J Biol Chem. 2003 May 30;278(22):20240-4. Epub 2003 Mar 20. PMID:12649270

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