This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2beo
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2beo.gif|left|200px]]<br /> | + | [[Image:2beo.gif|left|200px]]<br /><applet load="2beo" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2beo" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2beo, resolution 2.70Å" /> | caption="2beo, resolution 2.70Å" /> | ||
'''PRFA, TRANSCRIPTIONAL REGULATOR IN LISTERIA MONOCYTOGENES'''<br /> | '''PRFA, TRANSCRIPTIONAL REGULATOR IN LISTERIA MONOCYTOGENES'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BEO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with CL, GLN, PG4 and ACM as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2BEO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with CL, GLN, PG4 and ACM as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:GLN Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BEO OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 27: | ||
[[Category: virulence]] | [[Category: virulence]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:44:08 2007'' |
Revision as of 16:34, 18 December 2007
|
PRFA, TRANSCRIPTIONAL REGULATOR IN LISTERIA 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
2BEO is a Single protein structure of sequence from Listeria monocytogenes with CL, GLN, PG4 and ACM as ligands. Known structural/functional Site: . 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
Page seeded by OCA on Tue Dec 18 18:44:08 2007
