5zz5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:30, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5zz5' size='340' side='right'caption='[[5zz5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5zz5' size='340' side='right'caption='[[5zz5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5zz5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZZ5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5zz5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZZ5 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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&#8491;</td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zz5 OCA], [http://pdbe.org/5zz5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zz5 RCSB], [http://www.ebi.ac.uk/pdbsum/5zz5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zz5 ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5zz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zz5 OCA], [https://pdbe.org/5zz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zz5 RCSB], [https://www.ebi.ac.uk/pdbsum/5zz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zz5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/REX1_THEMA REX1_THEMA]] Modulates transcription in response to changes in cellular NADH/NAD(+) redox state.
+
[https://www.uniprot.org/uniprot/REX1_THEMA REX1_THEMA] Modulates transcription in response to changes in cellular NADH/NAD(+) redox state.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The cellular redox state of organisms continues to fluctuate during the metabolism. All organisms have various sensors that help detect and adapt to changes in the redox state. Nicotinamide adenine dinucleotides (NAD(+)/NADH), which are involved in various cellular metabolic activities as cofactors, have been revealed as the key molecules sensing the intra-cellular redox state. The Rex family members are well conserved transcriptional repressors that regulate the expression of respiratory genes by sensing the redox state according to the intra-cellular NAD(+)/NADH balance. Herein, we reported crystal structures of apo and NAD(+)- and NADH-bound forms of Rex from Thermotoga maritima to analyse the structural basis of transcriptional regulation depending on either NAD(+) or NADH binding. The different orientation of the reduced nicotinamide group to helix alpha9 caused the rearrangement of N-terminal DNA binding domain, thus resulting in closed form of Rex to dissociate from cognate DNA. The structural data of Rex from T. maritima also support the previous redox-sensing mechanism models of Rex homologues.
+
-
 
+
-
Structural Analysis of Redox-sensing Transcriptional Repressor Rex from Thermotoga maritima.,Park YW, Jang YY, Joo HK, Lee JY Sci Rep. 2018 Sep 5;8(1):13244. doi: 10.1038/s41598-018-31676-z. PMID:30185822<ref>PMID:30185822</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5zz5" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Jang, Y Y]]
+
[[Category: Thermotoga maritima MSB8]]
-
[[Category: Joo, H K]]
+
[[Category: Jang YY]]
-
[[Category: Lee, J Y]]
+
[[Category: Joo HK]]
-
[[Category: Park, Y W]]
+
[[Category: Lee JY]]
-
[[Category: Gene regulation]]
+
[[Category: Park YW]]
-
[[Category: Redox sensing]]
+
-
[[Category: Transcription factor]]
+

Current revision

Redox-sensing transcriptional repressor Rex

PDB ID 5zz5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5zz5"
Personal tools