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New page: '''Unreleased structure''' The entry 3djl is ON HOLD Authors: Eichman, B.F., Metz, A.H., Bowles, T. Description: Crystal structure of alkylation response protein E. coli AidB ''Page s...
 
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'''Unreleased structure'''


The entry 3djl is ON HOLD
==Crystal structure of alkylation response protein E. coli AidB==
<StructureSection load='3djl' size='340' side='right'caption='[[3djl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3djl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DJL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aidB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3djl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3djl OCA], [https://pdbe.org/3djl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3djl RCSB], [https://www.ebi.ac.uk/pdbsum/3djl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3djl ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/AIDB_ECOLI AIDB_ECOLI]] Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro.<ref>PMID:7961409</ref> <ref>PMID:16352838</ref> <ref>PMID:18829440</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dj/3djl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3djl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Exposure of Escherichia coli to alkylating agents activates expression of AidB in addition to DNA repair proteins Ada, AlkA, and AlkB. AidB was recently shown to possess a flavin adenine dinucleotide (FAD) cofactor and to bind to dsDNA, implicating it as a flavin-dependent DNA repair enzyme. However, the molecular mechanism by which AidB acts to reduce the mutagenic effects of specific DNA alkylators is unknown. We present a 1.7-A crystal structure of AidB, which bears superficial resemblance to the acyl-CoA dehydrogenase superfamily of flavoproteins. The structure reveals a unique quaternary organization and a distinctive FAD active site that provides a rationale for AidB's limited dehydrogenase activity. A highly electropositive C-terminal domain not present in structural homologs was identified by mutational analysis as the DNA binding site. Structural analysis of the DNA and FAD binding sites provides evidence against AidB-catalyzed DNA repair and supports a model in which AidB acts to prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target.


Authors: Eichman, B.F., Metz, A.H., Bowles, T.
Structure and DNA binding of alkylation response protein AidB.,Bowles T, Metz AH, O'Quin J, Wawrzak Z, Eichman BF Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15299-304. Epub 2008 Sep 30. PMID:18829440<ref>PMID:18829440</ref>


Description: Crystal structure of alkylation response protein E. coli AidB
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 13:08:06 2008''
<div class="pdbe-citations 3djl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Large Structures]]
[[Category: Bowles, T]]
[[Category: Eichman, B F]]
[[Category: Metz, A H]]
[[Category: Alpha helix]]
[[Category: Beta-barrel]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Oxidoreductase]]
Retrieved from "https://proteopedia.org/3djl"