4wai

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'''Unreleased structure'''
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==Structural characterization of the late competence protein ComFB from Bacillus subtilis.==
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<StructureSection load='4wai' size='340' side='right' caption='[[4wai]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4wai]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WAI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WAI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4wai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wai OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wai RCSB], [http://www.ebi.ac.uk/pdbsum/4wai PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Many bacteria take up DNA from their environment as part of the process of natural transformation. DNA uptake allows microorganisms to gain genetic diversity and can lead to the spread of antibiotic resistance or virulence genes within a microbial population. Development of genetic competence (Com) in Bacillus subtilis is a highly regulated process that culminates in expression of several late competence genes and formation of the DNA uptake apparatus. The late competence operon comF encodes a small protein of unknown function, ComFB. To gain insight into the function of ComFB, we determined its three-dimensional structure via X-ray crystallography. ComFB is a dimer, and each subunit consists of four alpha-helices connected by short loops and one extended beta-strand-like stretch. Each subunit contains one zinc-binding site formed by four cysteines, which are unusually spaced in the primary sequence. Using structure- and bioinformatics-guided substitutions we analyzed the intersubunit interface of the ComFB dimer. Based on these analyses, we conclude that ComFB is an obligate dimer. We also characterized ComFB in vivo and found that this protein is produced in competent cells and is localized to the cytosol. Consistent with previous reports, we showed that deletion of ComFB does not affect DNA uptake function. Combining our results, we conclude that ComFB is unlikely to be a part of the DNA uptake machinery under tested conditions and instead may have a regulatory function.
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The entry 4wai is ON HOLD until Paper Publication
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Structural characterization of the late competence protein ComFB from Bacillus subtilis.,Sysoeva TA, Bane LB, Xiao DY, Bose B, Chilton SS, Gaudet R, Burton BM Biosci Rep. 2014 Nov 21. PMID:25423369<ref>PMID:25423369</ref>
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Authors: Sysoeva, T.A., Bane, L.B., Xiao, D., Gaudet, R., Burton, B.M.
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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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Description: Structural characterization of the late competence protein ComFB from Bacillus subtilis.
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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: Bane, L B]]
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[[Category: Burton, B M]]
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[[Category: Gaudet, R]]
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[[Category: Sysoeva, T A]]
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[[Category: Xiao, D]]
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[[Category: Comf operon]]
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[[Category: Competent bacillus subtili]]
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[[Category: Dna uptake]]
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[[Category: Late competence operon]]
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[[Category: Natural transformation]]

Revision as of 16:01, 10 December 2014

Structural characterization of the late competence protein ComFB from Bacillus subtilis.

4wai, resolution 2.43Å

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