7bgs

<table><tr><td colspan='2'>[[7bgs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BGS FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

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== Publication Abstract from PubMed ==

This study describes the production, characterization and structure determination of a novel Holliday junction-resolving enzyme. The enzyme, termed Hjc_15-6, is encoded in the genome of phage Tth15-6, which infects Thermus thermophilus. Hjc_15-6 was heterologously produced in Escherichia coli and high yields of soluble and biologically active recombinant enzyme were obtained in both complex and defined media. Amino-acid sequence and structure comparison suggested that the enzyme belongs to a group of enzymes classified as archaeal Holliday junction-resolving enzymes, which are typically divalent metal ion-binding dimers that are able to cleave X-shaped dsDNA-Holliday junctions (Hjs). The crystal structure of Hjc_15-6 was determined to 2.5 A resolution using the selenomethionine single-wavelength anomalous dispersion method. To our knowledge, this is the first crystal structure of an Hj-resolving enzyme originating from a bacteriophage that can be classified as an archaeal type of Hj-resolving enzyme. As such, it represents a new fold for Hj-resolving enzymes from phages. Characterization of the structure of Hjc_15-6 suggests that it may form a dimer, or even a homodimer of dimers, and activity studies show endonuclease activity towards Hjs. Furthermore, based on sequence analysis it is proposed that Hjc_15-6 has a three-part catalytic motif corresponding to E-SD-EVK, and this motif may be common among other Hj-resolving enzymes originating from thermophilic bacteriophages.

Crystal structure and initial characterization of a novel archaeal-like Holliday junction-resolving enzyme from Thermus thermophilus phage Tth15-6.,Ahlqvist J, Linares-Pasten JA, Hakansson M, Jasilionis A, Kwiatkowska-Semrau K, Friethjonsson OH, Kaczorowska AK, Dabrowski S, AEvarsson A, Hreggviethsson GO, Al-Karadaghi S, Kaczorowski T, Nordberg Karlsson E Acta Crystallogr D Struct Biol. 2022 Feb 1;78(Pt 2):212-227. doi:, 10.1107/S2059798321012298. Epub 2022 Jan 24. PMID:35102887<ref>PMID:35102887</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 7bgs" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Ahlqvist, J]]

[[Category: Al-Karadaghi, S]]

[[Category: Hakansson, M]]

[[Category: Jasilionis, A]]

[[Category: Karlsson, E Nordberg]]

[[Category: Pasten, J A.Linares]]

[[Category: Archeal holliday junction resolvase helicase dna binding enzyme phage 15-6 thermus thermophilus]]

[[Category: Recombination]]