6imk: Difference between revisions

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-'''Unreleased structure'''
-The entry 6imk is ON HOLD
+==The crystal structure of AsfvLIG:CG complex==
+<StructureSection load='6imk' size='340' side='right'caption='[[6imk]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6imk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/African_swine_fever_virus African swine fever virus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IMK 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]] 2.502&#8491;</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=6imk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6imk OCA], [https://pdbe.org/6imk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6imk RCSB], [https://www.ebi.ac.uk/pdbsum/6imk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6imk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DNLI_ASFB7 DNLI_ASFB7] Very low-fidelity DNA ligase that seals nicks in double-stranded DNA during DNA repair (PubMed:15938630). Together with the viral repair DNA polymerase X, fills the single nucleotide gaps generated by the AP endonuclease (PubMed:15938630). It is not essential for viral replication and recombination (PubMed:15938630). Displays a very low adenylation activity towards DNA with 3'-dideoxy- or 3'-amino-terminated nicks compared to regular nick DNA (PubMed:15938630).<ref>PMID:15938630</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+African swine fever virus (ASFV) is contagious and can cause highly lethal disease in pigs. ASFV DNA ligase (AsfvLIG) is one of the most error-prone ligases identified to date; it catalyzes DNA joining reaction during DNA repair process of ASFV and plays important roles in mutagenesis of the viral genome. Here, we report four AsfvLIG:DNA complex structures and demonstrate that AsfvLIG has a unique N-terminal domain (NTD) that plays critical roles in substrate binding and catalytic complex assembly. In combination with mutagenesis, in vitro binding and catalytic assays, our study reveals that four unique active site residues (Asn153 and Leu211 of the AD domain; Leu402 and Gln403 of the OB domain) are crucial for the catalytic efficiency of AsfvLIG. These unique structural features can serve as potential targets for small molecule design, which could impair genome repair in ASFV and help combat this virus in the future.
-Authors:
+Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues.,Chen Y, Liu H, Yang C, Gao Y, Yu X, Chen X, Cui R, Zheng L, Li S, Li X, Ma J, Huang Z, Li J, Gan J Nat Commun. 2019 Jan 23;10(1):387. doi: 10.1038/s41467-019-08296-w. PMID:30674878<ref>PMID:30674878</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6imk" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[DNA ligase 3D structures|DNA ligase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: African swine fever virus]]
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Chen YQ]]
+[[Category: Gan JH]]