3bpv
From Proteopedia
(Difference between revisions)
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<StructureSection load='3bpv' size='340' side='right'caption='[[3bpv]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='3bpv' size='340' side='right'caption='[[3bpv]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3bpv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3bpv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_marburgensis_str._Marburg Methanothermobacter marburgensis str. Marburg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BPV FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpv OCA], [https://pdbe.org/3bpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpv RCSB], [https://www.ebi.ac.uk/pdbsum/3bpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpv 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=3bpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpv OCA], [https://pdbe.org/3bpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpv RCSB], [https://www.ebi.ac.uk/pdbsum/3bpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/O26413_METTH O26413_METTH] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bpv ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bpv ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Transcriptional regulators belonging to the MarR family are characterized by a winged-helix DNA binding domain. These transcriptional regulators regulate the efflux and influx of phenolic agents in bacteria and archaea. In Escherichia coli, MarR regulates the multiple antibiotic resistance operon and its inactivation produces a multiple antibiotic resistance phenotype. In some organisms, active efflux of drug compounds will produce a drug resistance phenotype, whereas in other organisms, active influx of chlorinated hydrocarbons results in their rapid degradation. Although proteins in the MarR family are regulators of important biological processes, their mechanism of action is not well understood and structural information about how phenolic agents regulate the activity of these proteins is lacking. This article presents the three-dimensional structure of a protein of the MarR family, MTH313, in its apo form and in complex with salicylate, a known inactivator. A comparison of these two structures indicates that the mechanism of regulation involves a large conformational change in the DNA binding lobe. Electrophoretic mobility shift assay and biophysical analyses further suggest that salicylate inactivates MTH313 and prevents it from binding to its promoter region. | ||
- | + | ==See Also== | |
- | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |
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- | == | + | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Methanothermobacter marburgensis str. Marburg]] |
- | [[Category: Christendat | + | [[Category: Christendat D]] |
- | [[Category: Saridakis | + | [[Category: Saridakis V]] |
- | [[Category: Shahinas | + | [[Category: Shahinas D]] |
- | [[Category: Xu | + | [[Category: Xu X]] |
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Current revision
Crystal Structure of MarR
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