5hm6: Difference between revisions
New page: '''Unreleased structure''' The entry 5hm6 is ON HOLD Authors: Roth, B.R., Davies, C. Description: N-terminal domain of BfmR from Acinetobacter baumannii [[Category: Unreleased Structur... |
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The | ==N-terminal domain of BfmR from Acinetobacter baumannii== | ||
<StructureSection load='5hm6' size='340' side='right'caption='[[5hm6]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hm6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HM6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hm6 OCA], [https://pdbe.org/5hm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hm6 RCSB], [https://www.ebi.ac.uk/pdbsum/5hm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hm6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q2VSW6_ACIBA Q2VSW6_ACIBA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The rise of drug-resistant bacterial infections coupled with decreasing antibiotic efficacy poses a significant challenge to global healthcare. Acinetobacter baumannii is an insidious, emerging bacterial pathogen responsible for severe nosocomial infections aided by its ability to form biofilms. The response regulator BfmR, from the BfmR/S two-component system, is the master regulator of biofilm initiation in A. baumannii and is a tractable therapeutic target. Here we present the structure of A. baumannii BfmR using a hybrid approach combining X-ray crystallography, nuclear magnetic resonance spectroscopy, chemical crosslinking mass spectrometry, and molecular modeling. We also show that BfmR binds the previously proposed bfmRS promoter sequence with moderate affinity. While BfmR shares many traits with other OmpR/PhoB family response regulators, some unusual properties were observed. Most importantly, we observe that when phosphorylated, BfmR binds this promoter sequence with a lower affinity than when not phosphorylated. All other OmpR/PhoB family members studied to date show an increase in DNA binding affinity upon phosphorylation. Understanding the structural and biochemical mechanisms of BfmR will aid in the development of new antimicrobial therapies. | |||
The structure of the biofilm-controlling response regulator BfmR from Acinetobacter baumannii reveals details of its DNA-binding mechanism.,Logan Draughn G, Milton ME, Feldmann EA, Bobay BG, Roth BM, Olson AL, Thompson RJ, Actis LA, Davies C, Cavanagh J J Mol Biol. 2018 Feb 10. pii: S0022-2836(18)30070-6. doi:, 10.1016/j.jmb.2018.02.002. PMID:29438671<ref>PMID:29438671</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Davies | <div class="pdbe-citations 5hm6" style="background-color:#fffaf0;"></div> | ||
[[Category: Roth | |||
==See Also== | |||
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acinetobacter baumannii]] | |||
[[Category: Large Structures]] | |||
[[Category: Davies C]] | |||
[[Category: Roth BR]] | |||
Latest revision as of 13:46, 16 August 2023
N-terminal domain of BfmR from Acinetobacter baumanniiN-terminal domain of BfmR from Acinetobacter baumannii
Structural highlights
FunctionPublication Abstract from PubMedThe rise of drug-resistant bacterial infections coupled with decreasing antibiotic efficacy poses a significant challenge to global healthcare. Acinetobacter baumannii is an insidious, emerging bacterial pathogen responsible for severe nosocomial infections aided by its ability to form biofilms. The response regulator BfmR, from the BfmR/S two-component system, is the master regulator of biofilm initiation in A. baumannii and is a tractable therapeutic target. Here we present the structure of A. baumannii BfmR using a hybrid approach combining X-ray crystallography, nuclear magnetic resonance spectroscopy, chemical crosslinking mass spectrometry, and molecular modeling. We also show that BfmR binds the previously proposed bfmRS promoter sequence with moderate affinity. While BfmR shares many traits with other OmpR/PhoB family response regulators, some unusual properties were observed. Most importantly, we observe that when phosphorylated, BfmR binds this promoter sequence with a lower affinity than when not phosphorylated. All other OmpR/PhoB family members studied to date show an increase in DNA binding affinity upon phosphorylation. Understanding the structural and biochemical mechanisms of BfmR will aid in the development of new antimicrobial therapies. The structure of the biofilm-controlling response regulator BfmR from Acinetobacter baumannii reveals details of its DNA-binding mechanism.,Logan Draughn G, Milton ME, Feldmann EA, Bobay BG, Roth BM, Olson AL, Thompson RJ, Actis LA, Davies C, Cavanagh J J Mol Biol. 2018 Feb 10. pii: S0022-2836(18)30070-6. doi:, 10.1016/j.jmb.2018.02.002. PMID:29438671[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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