5yej

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==Crystal structure of BioQ with its naturel double-stranded DNA operator==
==Crystal structure of BioQ with its naturel double-stranded DNA operator==
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<StructureSection load='5yej' size='340' side='right' caption='[[5yej]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='5yej' size='340' side='right'caption='[[5yej]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yej]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YEJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yej]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YEJ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEI_3111 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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]] 2.698&#8491;</td></tr>
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<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=5yej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yej OCA], [http://pdbe.org/5yej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yej RCSB], [http://www.ebi.ac.uk/pdbsum/5yej PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yej ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yej OCA], [https://pdbe.org/5yej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yej RCSB], [https://www.ebi.ac.uk/pdbsum/5yej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yej ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0QX69_MYCS2 A0QX69_MYCS2] TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.[ARBA:ARBA00002856]
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BACKGROUND: Biotin is an essential cofactor in living organisms. The TetR family transcriptional regulator (TFTR) BioQ is the main regulator of biotin synthesis in Mycobacterium smegmatis. BioQ represses the expression of its target genes by binding to a conserved palindromic DNA sequence (the BioQ operator). However, the mechanism by which BioQ recognizes this DNA element has not yet been fully elucidated. METHODS/RESULTS: We solved the crystal structures of the BioQ homodimer in its apo-form and in complex with its specific operator at 2.26A and 2.69A resolution, respectively. BioQ inserts the N-terminal recognition helix of each protomer into the corresponding major grooves of its operator and stabilizes the formation of the complex via electrostatic interactions and hydrogen bonding to induce conformational changes in both the DNA and BioQ. The DNA interface of BioQ is rich in positively charged residues, which help BioQ stabilize DNA binding. We elucidated the structural basis of DNA recognition by BioQ for the first time and identified the amino acid residues responsible for DNA binding via further site-directed mutagenesis. GENERAL SIGNIFICANCE: Our findings clearly elucidate the mechanism by which BioQ recognizes its operator in the biotin synthesis pathway and reveal the unique structural characteristics of BioQ that are distinct from other TFTR members.
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Structural insights into operator recognition by BioQ in the Mycobacterium smegmatis biotin synthesis pathway.,Yan L, Tang Q, Guan Z, Pei K, Zou T, He J Biochim Biophys Acta Gen Subj. 2018 Sep;1862(9):1843-1851. doi:, 10.1016/j.bbagen.2018.05.015. Epub 2018 May 28. PMID:29852200<ref>PMID:29852200</ref>
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==See Also==
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*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
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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 5yej" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mycs2]]
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[[Category: Large Structures]]
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[[Category: Guan, Z Y]]
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[[Category: Mycolicibacterium smegmatis MC2 155]]
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[[Category: Yan, L]]
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[[Category: Synthetic construct]]
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[[Category: Zou, T T]]
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[[Category: Guan ZY]]
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[[Category: Bioq]]
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[[Category: Yan L]]
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[[Category: Dna binding protein]]
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[[Category: Zou TT]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Dna complex]]
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[[Category: Tetr family]]
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Current revision

Crystal structure of BioQ with its naturel double-stranded DNA operator

PDB ID 5yej

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