6nx3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6nx3' size='340' side='right'caption='[[6nx3]], [[Resolution|resolution]] 1.87Å' scene=''> | <StructureSection load='6nx3' size='340' side='right'caption='[[6nx3]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6nx3]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NX3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6nx3]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Clope Clope]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NX3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPE0770 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195102 CLOPE])</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=6nx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nx3 OCA], [http://pdbe.org/6nx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nx3 RCSB], [http://www.ebi.ac.uk/pdbsum/6nx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nx3 ProSAT]</span></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=6nx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nx3 OCA], [http://pdbe.org/6nx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nx3 RCSB], [http://www.ebi.ac.uk/pdbsum/6nx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nx3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of BgaR, a transcriptional regulator of the lactose operon in Clostridium perfringens, has been solved by SAD phasing using a mercury derivative. BgaR is an exquisite sensor of lactose, with a binding affinity in the low-micromolar range. This sensor and regulator has been captured bound to lactose and to lactulose as well as in a nominal apo form, and was compared with AraC, another saccharide-binding transcriptional regulator. It is shown that the saccharides bind in the N-terminal region of a jelly-roll fold, but that part of the saccharide is exposed to bulk solvent. This differs from the classical AraC saccharide-binding site, which is mostly sequestered from the bulk solvent. The structures of BgaR bound to lactose and to lactulose highlight how specific and nonspecific interactions lead to a higher binding affinity of BgaR for lactose compared with lactulose. Moreover, solving multiple structures of BgaR in different space groups, both bound to saccharides and unbound, verified that the dimer interface along a C-terminal helix is similar to the dimer interface observed in AraC. | |||
Structures of the transcriptional regulator BgaR, a lactose sensor.,Newman J, Caron K, Nebl T, Peat TS Acta Crystallogr D Struct Biol. 2019 Jul 1;75(Pt 7):639-646. doi:, 10.1107/S2059798319008131. Epub 2019 Jun 26. PMID:31282473<ref>PMID:31282473</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6nx3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Clope]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Newman, J]] | [[Category: Newman, J]] | ||
Revision as of 11:40, 24 July 2019
Structures of the transcriptional regulator BgaR, a lactose sensor.Structures of the transcriptional regulator BgaR, a lactose sensor.
Structural highlights
Publication Abstract from PubMedThe structure of BgaR, a transcriptional regulator of the lactose operon in Clostridium perfringens, has been solved by SAD phasing using a mercury derivative. BgaR is an exquisite sensor of lactose, with a binding affinity in the low-micromolar range. This sensor and regulator has been captured bound to lactose and to lactulose as well as in a nominal apo form, and was compared with AraC, another saccharide-binding transcriptional regulator. It is shown that the saccharides bind in the N-terminal region of a jelly-roll fold, but that part of the saccharide is exposed to bulk solvent. This differs from the classical AraC saccharide-binding site, which is mostly sequestered from the bulk solvent. The structures of BgaR bound to lactose and to lactulose highlight how specific and nonspecific interactions lead to a higher binding affinity of BgaR for lactose compared with lactulose. Moreover, solving multiple structures of BgaR in different space groups, both bound to saccharides and unbound, verified that the dimer interface along a C-terminal helix is similar to the dimer interface observed in AraC. Structures of the transcriptional regulator BgaR, a lactose sensor.,Newman J, Caron K, Nebl T, Peat TS Acta Crystallogr D Struct Biol. 2019 Jul 1;75(Pt 7):639-646. doi:, 10.1107/S2059798319008131. Epub 2019 Jun 26. PMID:31282473[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||