3bzc

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Current revision (09:31, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3bzc' size='340' side='right'caption='[[3bzc]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
<StructureSection load='3bzc' size='340' side='right'caption='[[3bzc]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3bzc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BZC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3bzc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BZC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bzk|3bzk]]</div></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]] 2.27&#8491;</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=3bzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bzc OCA], [https://pdbe.org/3bzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bzc RCSB], [https://www.ebi.ac.uk/pdbsum/3bzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bzc 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=3bzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bzc OCA], [https://pdbe.org/3bzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bzc RCSB], [https://www.ebi.ac.uk/pdbsum/3bzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bzc ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9HTY8_PSEAE Q9HTY8_PSEAE]
== 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=3bzc 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=3bzc 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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Tex is a highly conserved bacterial protein that likely functions in a variety of transcriptional processes. Here, we describe two crystal structures of the 86-kDa Tex protein from Pseudomonas aeruginosa at 2.3 and 2.5 A resolution, respectively. These structures reveal a relatively flat and elongated protein, with several potential nucleic acid binding motifs clustered at one end, including an S1 domain near the C-terminus that displays considerable structural flexibility. Tex binds nucleic acids, with a preference for single-stranded RNA, and the Tex S1 domain is required for this binding activity. Point mutants further demonstrate that the primary nucleic acid binding site corresponds to a surface of the S1 domain. Sequence alignment and modeling indicate that the eukaryotic Spt6 transcription factor adopts a similar core structure. Structural analysis further suggests that the RNA polymerase and nucleosome interacting regions of Spt6 flank opposite sides of the Tex-like scaffold. Therefore, the Tex structure may represent a conserved scaffold that binds single-stranded RNA to regulate transcription in both eukaryotic and prokaryotic organisms.
 
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Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa.,Johnson SJ, Close D, Robinson H, Vallet-Gely I, Dove SL, Hill CP J Mol Biol. 2008 Apr 11;377(5):1460-73. Epub 2008 Feb 12. PMID:18321528<ref>PMID:18321528</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 3bzc" 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: Close, D]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Hill, C P]]
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[[Category: Close D]]
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[[Category: Johnson, S J]]
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[[Category: Hill CP]]
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[[Category: Helix-hairpin-helix]]
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[[Category: Johnson SJ]]
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[[Category: Helix-turn-helix]]
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[[Category: Rna binding protein]]
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[[Category: S1 domain]]
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[[Category: Transcription]]
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[[Category: Yqgf domain]]
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Current revision

Crystal Structure of the Tex protein from Pseudomonas aeruginosa, crystal form I

PDB ID 3bzc

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