1kgs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='1kgs' size='340' side='right'caption='[[1kgs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='1kgs' size='340' side='right'caption='[[1kgs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1kgs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KGS FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1kgs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KGS FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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]] 1.5&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DRRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=1kgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kgs OCA], [https://pdbe.org/1kgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kgs RCSB], [https://www.ebi.ac.uk/pdbsum/1kgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kgs ProSAT]</span></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=1kgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kgs OCA], [http://pdbe.org/1kgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kgs RCSB], [http://www.ebi.ac.uk/pdbsum/1kgs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kgs ProSAT]</span></td></tr>
+
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9WYN0_THEMA Q9WYN0_THEMA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 20:
</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=1kgs 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=1kgs ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
Two-component systems, the predominant signal transduction strategy used by prokaryotes, involve phosphorelay from a sensor histidine kinase (HK) to an intracellular response regulator protein (RR) that typically acts as a transcription regulator. RRs are modular proteins, usually composed of a conserved regulatory domain, which functions as a phosphorylation-activated switch, and an attached DNA binding effector domain. The crystal structure of a Thermotoga maritima transcription factor, DrrD, has been determined at 1.5 A resolution, providing the first structural information for a full-length member of the OmpR/PhoB subfamily of RRs. A small interdomain interface occurs between alpha 5 of the regulatory domain and an antiparallel sheet of the effector domain. The lack of an extensive interface in the unphosphorylated protein distinguishes DrrD from other structurally characterized multidomain RRs and suggests a different mode of interdomain regulation.
 
- 
-
Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima.,Buckler DR, Zhou Y, Stock AM Structure. 2002 Feb;10(2):153-64. PMID:11839301<ref>PMID:11839301</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1kgs" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Response regulator|Response regulator]]
*[[Response regulator|Response regulator]]
*[[Response regulator 3D structure|Response regulator 3D structure]]
*[[Response regulator 3D structure|Response regulator 3D structure]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Buckler, D R]]
+
[[Category: Thermotoga maritima]]
-
[[Category: Stock, A M]]
+
[[Category: Buckler DR]]
-
[[Category: Zhou, Y]]
+
[[Category: Stock AM]]
-
[[Category: Alph-beta sandwich]]
+
[[Category: Zhou Y]]
-
[[Category: Dna binding protein]]
+
-
[[Category: Dna-binding protein]]
+
-
[[Category: Helix-turn-helix]]
+
-
[[Category: Response regulator]]
+
-
[[Category: Winged-helix]]
+

Revision as of 08:00, 3 April 2024

Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima

PDB ID 1kgs

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools