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 1.60Å" /> '''The crystal structur...)
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Revision as of 00:54, 25 November 2007
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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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