6jyi: Difference between revisions

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'''Unreleased structure'''


The entry 6jyi is ON HOLD  until Paper Publication
==Crystal structure of the PadR-like transcriptional regulator BC1756 from Bacillus cereus==
<StructureSection load='6jyi' size='340' side='right'caption='[[6jyi]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jyi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JYI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JYI FirstGlance]. <br>
</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jyi OCA], [http://pdbe.org/6jyi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jyi RCSB], [http://www.ebi.ac.uk/pdbsum/6jyi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jyi ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transcription factors that belong to the PadR family play an essential role in the transcriptional regulation of diverse biological processes by recognizing their cognate palindromic DNA sequences. Bacillus cereus harbors a gene that encodes a PadR-like protein (bcPLP; BC1756). bcPLP has not been structurally characterized, and it remains unelucidated how bcPLP interacts with a specific DNA sequence to function as a transcription factor. To provide structural insights into DNA recognition by bcPLP, we performed a structural study and a DNA-binding analysis of bcPLP. The crystal structure of bcPLP was determined at 1.92A resolution. bcPLP consists of two domains, an N-terminal domain (NTD) and a C-terminal domain (CTD), and forms a homodimer mainly using the CTD. In the structure, bcPLP contains a highly positively charged elongated patch in the NTD that serves as a putative DNA-binding site. Indeed, an electrophoresis mobility shift assay and a fluorescence polarization assay showed that bcPLP specifically recognizes a palindromic DNA sequence upstream of the bcPLP-encoding region. Moreover, based on our mutagenesis and modeling studies, we demonstrate that bcPLP interacts with dsDNA primarily using the Y19, Y41, P64, and K66 residues in the NTD.


Authors:  
Structural and DNA-binding studies of the PadR-like transcriptional regulator BC1756 from Bacillus cereus.,Kim TH, Park SC, Lee KC, Song WS, Yoon SI Biochem Biophys Res Commun. 2019 Jun 6. pii: S0006-291X(19)31037-X. doi:, 10.1016/j.bbrc.2019.05.141. PMID:31178139<ref>PMID:31178139</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6jyi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Kim, T H]]
[[Category: Lee, K C]]
[[Category: Park, S C]]
[[Category: Song, W S]]
[[Category: Yoon, S I]]
[[Category: Transcription]]
[[Category: Transcription factor]]

Revision as of 06:54, 26 June 2019

Crystal structure of the PadR-like transcriptional regulator BC1756 from Bacillus cereus

6jyi, resolution 1.92Å

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