2mjg: Difference between revisions

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 ==Solution Structure of C-terminal AbrB==
-<StructureSection load='2mjg' size='340' side='right' caption='[[2mjg]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2mjg' size='340' side='right'caption='[[2mjg]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mjg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MJG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2mjg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJG FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">abrB, cpsX, BSU00370 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">abrB, cpsX, BSU00370 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjg OCA], [http://pdbe.org/2mjg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mjg RCSB], [http://www.ebi.ac.uk/pdbsum/2mjg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjg ProSAT]</span></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=2mjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjg OCA], [https://pdbe.org/2mjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mjg RCSB], [https://www.ebi.ac.uk/pdbsum/2mjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ABRB_BACSU ABRB_BACSU]] Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription.<ref>PMID:2504584</ref>
+[[https://www.uniprot.org/uniprot/ABRB_BACSU ABRB_BACSU]] Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription.<ref>PMID:2504584</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The AbrB protein from Bacillus subtilis is a DNA-binding global regulator controlling the onset of a vast array of protective functions under stressful conditions. Such functions include biofilm formation, antibiotic production, competence development, extracellular enzyme production, motility, and sporulation. AbrB orthologs are known in a variety of prokaryotic organisms, most notably in all infectious strains of Clostridia, Listeria, and Bacilli. Despite its central role in bacterial response and defense, its structure has been elusive because of its highly dynamic character. Orienting its N- and C-terminal domains with respect to one another has been especially problematic. Here, we have generated a structure of full-length, tetrameric AbrB using nuclear magnetic resonance, chemical crosslinking, and mass spectrometry. We note that AbrB possesses a strip of positive electrostatic potential encompassing its DNA-binding region and that its C-terminal domain aids in DNA binding.
+Structure and DNA-binding traits of the transition state regulator AbrB.,Olson AL, Tucker AT, Bobay BG, Soderblom EJ, Moseley MA, Thompson RJ, Cavanagh J Structure. 2014 Nov 4;22(11):1650-6. doi: 10.1016/j.str.2014.08.018. Epub 2014, Oct 9. PMID:25308864<ref>PMID:25308864</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2mjg" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
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 </StructureSection>
 [[Category: Bacsu]]
+[[Category: Large Structures]]
 [[Category: Cavanagh, J]]
 [[Category: Olson, A L]]