3ikt
From Proteopedia
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| - | {{STRUCTURE_3ikt|  PDB=3ikt  |  SCENE=  }}  | ||
| - | ===Crystal structure of a Rex-family repressor/DNA/NAD+ complex from Thermus aquaticus=== | ||
| - | {{ABSTRACT_PUBMED_20513431}} | ||
| - | == | + | ==Crystal structure of a Rex-family repressor/DNA/NAD+ complex from Thermus aquaticus== | 
| - | [[3ikt]] is a 4 chain structure with sequence from [ | + | <StructureSection load='3ikt' size='340' side='right'caption='[[3ikt]], [[Resolution|resolution]] 2.26Å' scene=''> | 
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ikt]] 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=3IKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IKT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=3ikt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ikt OCA], [https://pdbe.org/3ikt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ikt RCSB], [https://www.ebi.ac.uk/pdbsum/3ikt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ikt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + |   <jmolCheckbox> | ||
| + |     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ik/3ikt_consurf.spt"</scriptWhenChecked> | ||
| + |     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + |     <text>to colour the structure by Evolutionary Conservation</text> | ||
| + |   </jmolCheckbox> | ||
| + | </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=3ikt ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:20513431</ref> | |
| - | <ref  | + | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ikt" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Thermus thermophilus HB27]] | |
| - | + | [[Category: Kielkopf CL]] | |
| - | + | [[Category: McLaughlin KJ]] | |
| - | [[Category:  | + | |
| - | [[Category: Thermus  | + | |
| - | [[Category:  | + | |
| - | [[Category:  | + | |
| - | + | ||
Current revision
Crystal structure of a Rex-family repressor/DNA/NAD+ complex from Thermus aquaticus
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