2ewt

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Current revision (13:50, 13 March 2024) (edit) (undo)
 
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<StructureSection load='2ewt' size='340' side='right'caption='[[2ewt]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='2ewt' size='340' side='right'caption='[[2ewt]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ewt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EWT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ewt]] is a 1 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=2EWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EWT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2ewt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ewt OCA], [https://pdbe.org/2ewt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ewt RCSB], [https://www.ebi.ac.uk/pdbsum/2ewt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ewt ProSAT]</span></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=2ewt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ewt OCA], [https://pdbe.org/2ewt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ewt RCSB], [https://www.ebi.ac.uk/pdbsum/2ewt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ewt ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7AKQ8_STRCO Q7AKQ8_STRCO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2ewt 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=2ewt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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BldD is a central regulator of the developmental process in Streptomyces coelicolor. The 1.8 angstroms resolution structure of the DNA-binding domain of BldD (BldDN) reveals that BldDN forms a compact globular domain composed of four helices (alpha1-alpha4) containing a helix-turn-helix motif (alpha2-alpha3) resembling that of the DNA-binding domain of lambda repressor. The BldDN/DNA complex model led us to design a series of mutants, which revealed the important role of alpha3 and the 'turn' region between alpha2 and alpha3 for DNA recognition. Based on the fact that BldD occupies two operator sites of bldN and whiG and shows significant disparity in the affinity toward the two operator sites when they are disconnected, we propose a model of cooperative binding, which means that the binding of one BldD dimer to the high affinity site facilitates that of the second BldD dimer to the low affinity site. In addition, structural and mutational investigation reveals that the Tyr62Cys mutation, found in the first-identified bldD mutant, can destabilize BldD structure by disrupting the hydrophobic core.
 
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Crystal structure of the DNA-binding domain of BldD, a central regulator of aerial mycelium formation in Streptomyces coelicolor A3(2).,Kim IK, Lee CJ, Kim MK, Kim JM, Kim JH, Yim HS, Cha SS, Kang SO Mol Microbiol. 2006 Jun;60(5):1179-93. PMID:16689794<ref>PMID:16689794</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2ewt" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Strco]]
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[[Category: Cha SS]]
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[[Category: Cha, S S]]
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[[Category: Kang SO]]
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[[Category: Kang, S O]]
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[[Category: Kim IK]]
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[[Category: Kim, I K]]
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[[Category: Kim JH]]
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[[Category: Kim, J H]]
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[[Category: Kim JM]]
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[[Category: Kim, J M]]
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[[Category: Kim MK]]
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[[Category: Kim, M K]]
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[[Category: Lee CJ]]
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[[Category: Lee, C J]]
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[[Category: Yim HS]]
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[[Category: Yim, H S]]
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[[Category: Dna binding protein]]
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[[Category: The dna-binding domain of bldd]]
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Current revision

Crystal structure of the DNA-binding domain of BldD

PDB ID 2ewt

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