View source for 8ain


==MCUGI SAUNG complex==
<StructureSection load='8ain' size='340' side='right'caption='[[8ain]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ain]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Macrococcus_caseolyticus Macrococcus caseolyticus] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIN 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8ain FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ain OCA], [https://pdbe.org/8ain PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ain RCSB], [https://www.ebi.ac.uk/pdbsum/8ain PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ain ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
DNA-mimicking proteins encoded by viruses can modulate processes such as innate cellular immunity. An example is Ung-family uracil-DNA glycosylase inhibition, which prevents Ung-mediated degradation via the stoichiometric protein blockade of the Ung DNA-binding cleft. This is significant where uracil-DNA is a key determinant in the replication and distribution of virus genomes. Unrelated protein folds support a common physicochemical spatial strategy for Ung inhibition, characterised by pronounced sequence plasticity within the diverse fold families. That, and the fact that relatively few template sequences are biochemically verified to encode Ung inhibitor proteins, presents a barrier to the straightforward identification of Ung inhibitors in genomic sequences. In this study, distant homologs of known Ung inhibitors were characterised via structural biology and structure prediction methods. A recombinant cellular survival assay and in vitro biochemical assay were used to screen distant variants and mutants to further explore tolerated sequence plasticity in motifs supporting Ung inhibition. The resulting validated sequence repertoire defines an expanded set of heuristic sequence and biophysical signatures shared by known Ung inhibitor proteins. A computational search of genome database sequences and the results of recombinant tests of selected output sequences obtained are presented here.

A Multimodal Approach towards Genomic Identification of Protein Inhibitors of Uracil-DNA Glycosylase.,Muselmani W, Kashif-Khan N, Bagneris C, Santangelo R, Williams MA, Savva R Viruses. 2023 Jun 10;15(6):1348. doi: 10.3390/v15061348. PMID:37376646<ref>PMID:37376646</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ain" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Macrococcus caseolyticus]]
[[Category: Staphylococcus aureus]]
[[Category: Muselmani W]]
[[Category: Savva R]]