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| - | [[Image:2beo.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2beo| PDB=2beo | SCENE= }} | | {{STRUCTURE_2beo| PDB=2beo | SCENE= }} |
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| - | '''PRFA, TRANSCRIPTIONAL REGULATOR IN LISTERIA MONOCYTOGENES'''
| + | ===PRFA, TRANSCRIPTIONAL REGULATOR IN LISTERIA MONOCYTOGENES=== |
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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15813735}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15813735 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15813735}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Transcriptional regulator]] | | [[Category: Transcriptional regulator]] |
| | [[Category: Virulence]] | | [[Category: Virulence]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:11:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:36:55 2008'' |
Revision as of 21:37, 27 July 2008
Template:STRUCTURE 2beo
PRFA, TRANSCRIPTIONAL REGULATOR IN LISTERIA MONOCYTOGENES
Template:ABSTRACT PUBMED 15813735
About this Structure
2BEO 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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