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| | <StructureSection load='3il2' size='340' side='right'caption='[[3il2]], [[Resolution|resolution]] 2.49Å' scene=''> | | <StructureSection load='3il2' size='340' side='right'caption='[[3il2]], [[Resolution|resolution]] 2.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3il2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IL2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3il2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IL2 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xcb|1xcb]], [[3ikt|3ikt]], [[3ikv|3ikv]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rex, TT_C1293 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=3il2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3il2 OCA], [https://pdbe.org/3il2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3il2 RCSB], [https://www.ebi.ac.uk/pdbsum/3il2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3il2 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=3il2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3il2 OCA], [https://pdbe.org/3il2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3il2 RCSB], [https://www.ebi.ac.uk/pdbsum/3il2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3il2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/REX_THET2 REX_THET2]] Modulates transcription in response to changes in cellular NADH/NAD(+) redox state (By similarity).
| + | [https://www.uniprot.org/uniprot/REX_THET2 REX_THET2] Modulates transcription in response to changes in cellular NADH/NAD(+) redox state (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet2]] | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Kielkopf, C L]] | + | [[Category: Kielkopf CL]] |
| - | [[Category: McLaughlin, K J]] | + | [[Category: McLaughlin KJ]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Nicotinamide adenine dinucleotide]]
| + | |
| - | [[Category: Redox-sensing]]
| + | |
| - | [[Category: Repressor]]
| + | |
| - | [[Category: Rex]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Thermus aquaticus]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Winged helix]]
| + | |
| Structural highlights
Function
REX_THET2 Modulates transcription in response to changes in cellular NADH/NAD(+) redox state (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Nicotinamide adenine dinucleotides have emerged as key signals of the cellular redox state. Yet the structural basis for allosteric gene regulation by the ratio of reduced NADH to oxidized NAD(+) is poorly understood. A key sensor among Gram-positive bacteria, Rex represses alternative respiratory gene expression until a limited oxygen supply elevates the intracellular NADH:NAD(+) ratio. Here we investigate the molecular mechanism for NADH/NAD(+) sensing among Rex family members by determining structures of Thermus aquaticus Rex bound to (1) NAD(+), (2) DNA operator, and (3) without ligand. Comparison with the Rex/NADH complex reveals that NADH releases Rex from the DNA site following a 40 degrees closure between the dimeric subunits. Complementary site-directed mutagenesis experiments implicate highly conserved residues in NAD-responsive DNA-binding activity. These rare views of a redox sensor in action establish a means for slight differences in the nicotinamide charge, pucker, and orientation to signal the redox state of the cell.
Structural basis for NADH/NAD+ redox sensing by a Rex family repressor.,McLaughlin KJ, Strain-Damerell CM, Xie K, Brekasis D, Soares AS, Paget MS, Kielkopf CL Mol Cell. 2010 May 28;38(4):563-75. PMID:20513431[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McLaughlin KJ, Strain-Damerell CM, Xie K, Brekasis D, Soares AS, Paget MS, Kielkopf CL. Structural basis for NADH/NAD+ redox sensing by a Rex family repressor. Mol Cell. 2010 May 28;38(4):563-75. PMID:20513431 doi:10.1016/j.molcel.2010.05.006
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