2bgc: Difference between revisions

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[[Image:2bgc.gif|left|200px]]
{{Seed}}
[[Image:2bgc.png|left|200px]]


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{{STRUCTURE_2bgc|  PDB=2bgc  |  SCENE=  }}  
{{STRUCTURE_2bgc|  PDB=2bgc  |  SCENE=  }}  


'''PRFA-G145S, A CONSTITUTIVE ACTIVE MUTANT OF THE TRANSCRIPTIONAL REGULATOR IN L.MONOCYTOGENES'''
===PRFA-G145S, A CONSTITUTIVE ACTIVE MUTANT OF THE TRANSCRIPTIONAL REGULATOR IN L.MONOCYTOGENES===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15813735}}


==About this Structure==
==About this Structure==
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[[Category: Schubert, W D.]]
[[Category: Schubert, W D.]]
[[Category: Bacterial infection,human pathogen,transcriptional regulator,transcription]]
[[Category: Bacterial infection,human pathogen,transcriptional regulator,transcription]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:14:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:01:18 2008''

Revision as of 09:01, 29 July 2008

File:2bgc.png

Template:STRUCTURE 2bgc

PRFA-G145S, A CONSTITUTIVE ACTIVE MUTANT OF THE TRANSCRIPTIONAL REGULATOR IN L.MONOCYTOGENES

Template:ABSTRACT PUBMED 15813735

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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