8dfk

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'''Unreleased structure'''
 
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The entry 8dfk is ON HOLD until Paper Publication
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==X-ray crystal structure of Bacillus subtilis ComEA==
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<StructureSection load='8dfk' size='340' side='right'caption='[[8dfk]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8dfk]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DFK FirstGlance]. <br>
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</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=8dfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dfk OCA], [https://pdbe.org/8dfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dfk RCSB], [https://www.ebi.ac.uk/pdbsum/8dfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dfk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/COMEA_BACSU COMEA_BACSU] Needed for both DNA binding and transport. It is absolutely required for the uptake of transforming DNA but not for binding. Its role in binding may be indirect.<ref>PMID:7968523</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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An essential step in bacterial transformation is the uptake of DNA into the periplasm, across the thick peptidoglycan cell wall of Gram-positive bacteria, or the outer membrane and thin peptidoglycan layer of Gram-negative bacteria. ComEA, a DNA-binding protein widely conserved in transformable bacteria, is required for this uptake step. Here we determine X-ray crystal structures of ComEA from two Gram-positive species, Bacillus subtilis and Geobacillus stearothermophilus, identifying a domain that is absent in Gram-negative bacteria. X-ray crystallographic, genetic, and analytical ultracentrifugation (AUC) analyses reveal that this domain drives ComEA oligomerization, which we show is required for transformation. We use multi-wavelength AUC (MW-AUC) to characterize the interaction between DNA and the ComEA DNA-binding domain. Finally, we present a model for the interaction of the ComEA DNA-binding domain with DNA, suggesting that ComEA oligomerization may provide a pulling force that drives DNA uptake across the thick cell walls of Gram-positive bacteria.
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Authors:
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Structure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria.,Ahmed I, Hahn J, Henrickson A, Khaja FT, Demeler B, Dubnau D, Neiditch MB Nat Commun. 2022 Dec 13;13(1):7724. doi: 10.1038/s41467-022-35129-0. PMID:36513643<ref>PMID:36513643</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8dfk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
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[[Category: Large Structures]]
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[[Category: Ahmed I]]
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[[Category: Khaja FT]]
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[[Category: Neiditch MB]]

Revision as of 09:10, 28 December 2022

X-ray crystal structure of Bacillus subtilis ComEA

PDB ID 8dfk

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