2lzf: Difference between revisions
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==Structure of the biofilm matrix promoter AbbA from B. subtilis== | |||
<StructureSection load='2lzf' size='340' side='right'caption='[[2lzf]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lzf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LZF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lzf OCA], [https://pdbe.org/2lzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lzf RCSB], [https://www.ebi.ac.uk/pdbsum/2lzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lzf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/YKZF_BACSU YKZF_BACSU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteria respond to adverse environmental conditions by switching on the expression of large numbers of genes that enable them to adapt to unfavorable circumstances. In Bacillus subtilis, many adaptive genes are under the negative control of the global transition state regulator, the repressor protein AbrB. Stressful conditions lead to the de-repression of genes under AbrB control. Contributing to this de-repression is AbbA, an anti-repressor that binds to and blocks AbrB from binding to DNA. Here, we have determined the NMR structure of the functional AbbA dimer, confirmed that it binds to the N-terminal DNA-binding domain of AbrB, and have provided an initial description for the interaction using computational docking procedures. Interestingly, we show that AbbA has structural and surface characteristics that closely mimic the DNA phosphate backbone, enabling it to readily carry out its physiological function. | |||
A DNA Mimic: The Structure and Mechanism of Action for the Anti-Repressor Protein AbbA.,Tucker AT, Bobay BG, Banse AV, Olson AL, Soderblom EJ, Moseley MA, Thompson RJ, Varney KM, Losick R, Cavanagh J J Mol Biol. 2014 Feb 15. pii: S0022-2836(14)00077-1. doi:, 10.1016/j.jmb.2014.02.010. PMID:24534728<ref>PMID:24534728</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lzf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis subsp. subtilis str. 168]] | |||
[[Category: Large Structures]] | |||
[[Category: Bobay BG]] | |||
[[Category: Cavanagh J]] | |||
[[Category: Losick R]] | |||
[[Category: Tucker AT]] | |||