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| - | [[Image:2z69.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2z69| PDB=2z69 | SCENE= }} | | {{STRUCTURE_2z69| PDB=2z69 | SCENE= }} |
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| - | '''Crystal Structure of the sensor domain of the transcriptional regulator DNR from Pseudomonas aeruginosa'''
| + | ===Crystal Structure of the sensor domain of the transcriptional regulator DNR from Pseudomonas aeruginosa=== |
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| - | ==Overview==
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| - | All denitrifying bacteria can keep the steady-state concentrations of nitrite and nitric oxide (NO) below cytotoxic levels, controlling the expression of the denitrification gene clusters by redox signaling, mainly through transcriptional regulators belonging either to the DNR (dissimilative nitrate respiration regulator) or to the NnrR (nitrite and nitric oxide reductase regulator) subgroups of the FNR (fumarate and nitrate reductase regulatory protein)-CRP (cAMP receptor protein) superfamily. The NO dependence of the transcriptional activity of promoters regulated by these transcription factors has suggested that they may act as NO sensors in vivo. Despite great interest in the regulation of denitrification, which in Pseudomonas aeruginosa is strictly related to virulence, functional and structural characterization of these NO sensors is still lacking. Here we present the three-dimensional structure of the sensor domain of the DNR from P. aeruginosa at 2.1 A resolution. This is the first structure of a putative NO-sensing bacterial transcriptional regulator and reveals the presence of a large hydrophobic cavity that may be the cofactor binding site. Parallel spectroscopic evidence indicates that apo-DNR binds heme in vitro and that the heme-bound form reacts with carbon monoxide and NO, thus supporting the hypothesis that NO sensing involves gas binding to the ferrous heme. Preliminary experiments indicate that heterologous expression of the heme-containing DNR yields a protein able to bind DNA in vitro.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18420222}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18420222 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18420222}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Dimerization helix]] | | [[Category: Dimerization helix]] |
| | [[Category: Transcription regulator]] | | [[Category: Transcription regulator]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:59:59 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:23:43 2008'' |
Revision as of 21:23, 28 July 2008
Template:STRUCTURE 2z69
Crystal Structure of the sensor domain of the transcriptional regulator DNR from Pseudomonas aeruginosa
Template:ABSTRACT PUBMED 18420222
About this Structure
2Z69 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
NO sensing in Pseudomonas aeruginosa: structure of the transcriptional regulator DNR., Giardina G, Rinaldo S, Johnson KA, Di Matteo A, Brunori M, Cutruzzola F, J Mol Biol. 2008 May 16;378(5):1002-15. Epub 2008 Mar 14. PMID:18420222
Page seeded by OCA on Tue Jul 29 00:23:43 2008
