2bgc
From Proteopedia
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| - | [[Image:2bgc.gif|left|200px]] | + | [[Image:2bgc.gif|left|200px]] |
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| - | '''PRFA-G145S, A CONSTITUTIVE ACTIVE MUTANT OF THE TRANSCRIPTIONAL REGULATOR IN L.MONOCYTOGENES''' | + | {{Structure |
| + | |PDB= 2bgc |SIZE=350|CAPTION= <scene name='initialview01'>2bgc</scene>, resolution 2.30Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Dtt+Binding+Site+For+Chain+F'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene> and <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PRFA-G145S, A CONSTITUTIVE ACTIVE MUTANT OF THE TRANSCRIPTIONAL REGULATOR IN L.MONOCYTOGENES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BGC is a [ | + | 2BGC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BGC OCA]. |
==Reference== | ==Reference== | ||
| - | The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif., Eiting M, Hageluken G, Schubert WD, Heinz DW, Mol Microbiol. 2005 Apr;56(2):433-46. PMID:[http:// | + | The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif., Eiting M, Hageluken G, Schubert WD, Heinz DW, Mol Microbiol. 2005 Apr;56(2):433-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15813735 15813735] |
[[Category: Listeria monocytogenes]] | [[Category: Listeria monocytogenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcriptional regulator]] | [[Category: transcriptional regulator]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:32 2008'' |
Revision as of 14:01, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
PRFA-G145S, A CONSTITUTIVE ACTIVE MUTANT OF THE TRANSCRIPTIONAL REGULATOR IN L.MONOCYTOGENES
Overview
Listeria monocytogenes, a Gram-positive, facultative intracellular human pathogen, causes systemic infections with high mortality rate. The majority of the known pathogenicity factors of L. monocytogenes is regulated by a single transcription factor, PrfA. Hyperhaemolytic laboratory strains of L. monocytogenes express the constitutively active mutant PrfA(G145S) inducing virulence gene overexpression independent of environmental conditions. PrfA belongs to the Crp/Fnr family of transcription factors generally activated by a small effector, such as cAMP or O(2). We present the crystal structures of wild-type PrfA, the first Gram-positive member of the Crp/Fnr family, and of the constitutively active mutant PrfA(G145S). Cap (Crp) has previously been described exclusively in the cAMP-induced (DNA-free and -bound) conformation. By contrast, the PrfA structures present views both of the non-induced state and of the mutationally activated form. The low DNA-binding affinity of wild-type PrfA is supported both structurally (partly disordered helix-turn-helix motif, overall geometry of the HTH alpha-helices deviates from Cap) and by surface plasmon resonance analyses (K(D) = 0.9 microM). In PrfA(G145S) the HTH motifs dramatically rearrange to adopt a conformation comparable to cAMP-induced Cap and hence favourable for DNA binding, supported by a DNA-binding affinity of 50 nM. Finally, the hypothesis that wild-type PrfA, like other Crp/Fnr family members, may require an as yet unidentified cofactor for activation is supported by the presence of a distinct tunnel in PrfA, located at the interface of the beta-barrel and the DNA-binding domain.
About this Structure
2BGC is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.
Reference
The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif., Eiting M, Hageluken G, Schubert WD, Heinz DW, Mol Microbiol. 2005 Apr;56(2):433-46. PMID:15813735
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