View source for 9zd6


==Bacterial interstrand DNA crosslink glycosylase AlkX/YcaQ bound to DNA==
<StructureSection load='9zd6' size='340' side='right'caption='[[9zd6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9zd6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/DNA_molecule DNA molecule] and [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ZD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ZD6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=9zd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9zd6 OCA], [https://pdbe.org/9zd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9zd6 RCSB], [https://www.ebi.ac.uk/pdbsum/9zd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9zd6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q47TC5_THEFY Q47TC5_THEFY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interstrand DNA crosslinks (ICLs) are a highly toxic form of DNA damage. ICL repair in both eukaryotes and bacteria involves unhooking of the two strands by specialized DNA glycosylases. We recently established that the human pathogen Acinetobacter baumannii contains an ICL glycosylase (AlkX) that facilitates pathogenesis and protects the bacteria from DNA damage and acid stress. However, the physical basis for glycosylase-catalyzed ICL unhooking is unknown. Here, we describe a crystal structure of AlkX bound to DNA representing a product of the ICL unhooking reaction. Mutational analysis of ICL unhooking in vitro and A. baumannii sensitivity to the crosslinking agent mechlorethamine enabled identification of several AlkX motifs critical for ICL repair. We also found that a genetic variant from an antibiotic-resistant strain of the human pathogen Salmonella enterica significantly reduced AlkX activity in vitro and increased A. baumannii sensitivity to DNA crosslinking. This work provides a structural basis for how bacterial ICL glycosylases recognize and repair DNA adducts and contributes additional evidence that ICL repair is important for fitness of human pathogens.

DNA binding and lesion recognition by the bacterial interstrand DNA crosslink glycosylase AlkX.,Cai è¡æ¯å¨ Y, Kunkle DE, Edinbugh MD, Skaar EP, Eichman BF bioRxiv [Preprint]. 2025 Dec 13:2025.12.11.693820. doi: , 10.64898/2025.12.11.693820. PMID:41427321<ref>PMID:41427321</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9zd6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: DNA molecule]]
[[Category: Large Structures]]
[[Category: Thermobifida fusca]]
[[Category: Cai Y]]
[[Category: Eichman BF]]