3ih2: Difference between revisions
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==TM1030 crystallized at 323K== | ==TM1030 crystallized at 323K== | ||
<StructureSection load='3ih2' size='340' side='right' caption='[[3ih2]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3ih2' size='340' side='right'caption='[[3ih2]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ih2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ih2]] 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=3IH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IH2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ih2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ih2 OCA], [https://pdbe.org/3ih2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ih2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ih2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ih2 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9X0C0_THEMA Q9X0C0_THEMA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 14: | Line 15: | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/3ih2_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/3ih2_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 28: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 3ih2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3ih2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bujacz | [[Category: Thermotoga maritima]] | ||
[[Category: Chruszcz | [[Category: Bujacz G]] | ||
[[Category: Joachimiak | [[Category: Chruszcz M]] | ||
[[Category: Koclega | [[Category: Joachimiak A]] | ||
[[Category: Koclega KD]] | |||
[[Category: Minor | [[Category: Minor W]] | ||
Latest revision as of 04:57, 21 November 2024
TM1030 crystallized at 323KTM1030 crystallized at 323K
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTranscriptional regulator protein TM1030 from the hyperthermophile Thermotoga maritima, as well as its complex with DNA, was crystallized at a wide range of temperatures. Crystallization plates were incubated at 4, 20, 37 and 50 degrees C over 3 weeks. The best crystals of TM1030 in complex with DNA were obtained at 4, 20 and 37 degrees C, while TM1030 alone crystallized almost equally well in all temperatures. The crystals grown at different temperatures were used for X-ray diffraction experiments and their structures were compared. Surprisingly, the models of TM1030 obtained from crystals grown at different temperatures are similar in quality. While there are some examples of structures of proteins grown at elevated temperatures in the PDB, these temperatures appear to be underrepresented. Our studies show that crystals of some proteins may be grown and are stable at broad range of temperatures. We suggest that crystallization experiments at elevated temperatures could be used as a standard part of the crystallization protocol. 'Hot' macromolecular crystals.,Koclega KD, Chruszcz M, Zimmerman MD, Bujacz G, Minor W Cryst Growth Des. 2009 Dec 18;10(2):580. PMID:20161694[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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