View source for 2naz


==The solution NMR structure of the C-terminal effector domain of BfmR from Acinetobacter baumannii==
<StructureSection load='2naz' size='340' side='right'caption='[[2naz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2naz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ATCC_19606_=_CIP_70.34_=_JCM_6841 Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NAZ FirstGlance]. <br>
</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=2naz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2naz OCA], [https://pdbe.org/2naz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2naz RCSB], [https://www.ebi.ac.uk/pdbsum/2naz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2naz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D0C9D6_ACIB2 D0C9D6_ACIB2] 
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Acinetobacter baumannii ATCC 19606 = CIP 70 34 = JCM 6841]]
[[Category: Large Structures]]
[[Category: Bobay BG]]
[[Category: Cavanagh J]]
[[Category: Feldmann EA]]
[[Category: Olson AL]]
[[Category: Thompson RJ]]