2q24: Difference between revisions
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< | ==Crystal structure of TetR transcriptional regulator SCO0520 from Streptomyces coelicolor== | ||
<StructureSection load='2q24' size='340' side='right'caption='[[2q24]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2q24]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q24 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2q24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q24 OCA], [https://pdbe.org/2q24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q24 RCSB], [https://www.ebi.ac.uk/pdbsum/2q24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q24 ProSAT], [https://www.topsan.org/Proteins/MCSG/2q24 TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9RJL5_STRCO Q9RJL5_STRCO] | |||
== 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/q2/2q24_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2q24 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 A resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an ohm-shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function. | |||
Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins.,Filippova EV, Chruszcz M, Cymborowski M, Gu J, Savchenko A, Edwards A, Minor W J Struct Funct Genomics. 2011 May 29. PMID:21625866<ref>PMID:21625866</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2q24" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: Chruszcz | <references/> | ||
[[Category: Cymborowski | __TOC__ | ||
[[Category: Edwards | </StructureSection> | ||
[[Category: Filippova | [[Category: Large Structures]] | ||
[[Category: Gu | [[Category: Chruszcz M]] | ||
[[Category: Joachimiak | [[Category: Cymborowski M]] | ||
[[Category: Koclega | [[Category: Edwards AM]] | ||
[[Category: Filippova EV]] | |||
[[Category: Minor | [[Category: Gu J]] | ||
[[Category: Savchenko | [[Category: Joachimiak A]] | ||
[[Category: Xu | [[Category: Koclega KD]] | ||
[[Category: Minor W]] | |||
[[Category: Savchenko A]] | |||
[[Category: Xu X]] | |||
Latest revision as of 04:20, 21 November 2024
Crystal structure of TetR transcriptional regulator SCO0520 from Streptomyces coelicolorCrystal structure of TetR transcriptional regulator SCO0520 from Streptomyces coelicolor
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 PubMedA structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 A resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an ohm-shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function. Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins.,Filippova EV, Chruszcz M, Cymborowski M, Gu J, Savchenko A, Edwards A, Minor W J Struct Funct Genomics. 2011 May 29. PMID:21625866[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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