1utx
From Proteopedia
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| - | [[Image:1utx.jpg|left|200px]]<br /><applet load="1utx" size=" | + | [[Image:1utx.jpg|left|200px]]<br /><applet load="1utx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1utx, resolution 1.90Å" /> | caption="1utx, resolution 1.90Å" /> | ||
'''REGULATION OF CYTOLYSIN EXPRESSION BY ENTEROCOCCUS FAECALIS: ROLE OF CYLR2'''<br /> | '''REGULATION OF CYTOLYSIN EXPRESSION BY ENTEROCOCCUS FAECALIS: ROLE OF CYLR2'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UTX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with IOD and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Na Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1UTX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with <scene name='pdbligand=IOD:'>IOD</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcriptional repressor]] | [[Category: transcriptional repressor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:04:54 2008'' |
Revision as of 08:04, 3 February 2008
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REGULATION OF CYTOLYSIN EXPRESSION BY ENTEROCOCCUS FAECALIS: ROLE OF CYLR2
Overview
Enterococcus faecalis is one of the major causes for hospital-acquired, antibiotic-resistant infections. It produces an exotoxin, called, cytolysin, which is lethal for a wide range of Gram-positive bacteria and, is toxic to higher organisms. Recently, the regulation of the cytolysin, operon was connected to autoinduction by a quorum-sensing mechanism, involving the CylR1/CylR2 two-component regulatory system. We report here, the crystal structure of CylR2 and its properties in solution as, determined by heteronuclear NMR spectroscopy. The structure reveals a, rigid dimer containing a helix-turn-helix DNA-binding motif as part of a, five-helix bundle that is extended by an antiparallel beta-sheet. We show, that CylR2 is a DNA-binding protein that binds specifically to a 22 bp, fragment of the cytolysin promoter region. NMR chemical shift perturbation, experiments identify surfaces involved in DNA binding and are in agreement, with a model for the CylR2/DNA complex that attributes binding specificity, to a complex network of CylR2/DNA interactions. Our results propose a, mechanism where repression is achieved by CylR2 obstruction of the, promoter preventing biosynthesis of the cytolysin operon transcript.
About this Structure
1UTX is a Single protein structure of sequence from Enterococcus faecalis with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis., Rumpel S, Razeto A, Pillar CM, Vijayan V, Taylor A, Giller K, Gilmore MS, Becker S, Zweckstetter M, EMBO J. 2004 Sep 15;23(18):3632-42. Epub 2004 Sep 9. PMID:15359276
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