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5h0m

From Proteopedia

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<StructureSection load='5h0m' size='340' side='right'caption='[[5h0m]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
<StructureSection load='5h0m' size='340' side='right'caption='[[5h0m]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5h0m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_gsve2 Bacteriophage gsve2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H0M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H0M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5h0m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_virus_E2 Geobacillus virus E2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H0M FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h0o|5h0o]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h0m OCA], [http://pdbe.org/5h0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h0m RCSB], [http://www.ebi.ac.uk/pdbsum/5h0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h0m ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h0m OCA], [https://pdbe.org/5h0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h0m RCSB], [https://www.ebi.ac.uk/pdbsum/5h0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h0m ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1U7Q1S7_9CAUD A0A1U7Q1S7_9CAUD]
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HNH endonucleases in bacteriophages play a variety of roles in the phage lifecycle as key components of phage DNA packaging machines. The deep-sea thermophilic bacteriophage Geobacillus virus E2 (GVE2) encodes an HNH endonuclease (GVE2 HNHE). Here, the crystal structure of GVE2 HNHE is reported. This is the first structural study of a thermostable HNH endonuclease from a thermophilic bacteriophage. Structural comparison reveals that GVE2 HNHE possesses a typical betabetaalpha-metal fold and Zn-finger motif similar to those of HNH endonucleases from other bacteriophages, apart from containing an extra alpha-helix, suggesting conservation of these enzymes among bacteriophages. Biochemical analysis suggests that the alanine substitutions of the conserved residues (H93, N109 and H118) in the HNH motif of GVE2 HNHE abolished 94%, 60% and 83% of nicking activity, respectively. Compared to the wild type enzyme, the H93A mutant displayed almost the same conformation while the N108A and H118A mutants had different conformations. In addition, the wild type enzyme was more thermostable than the mutants. In the presence of Mn2+ or Zn2+, the wild type enzyme displayed distinct DNA nicking patterns. However, high Mn2+ concentrations were needed for the N109A and H118A mutants to nick DNA while Zn2+ inactivated their nicking activity.
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Structural and functional characterization of deep-sea thermophilic bacteriophage GVE2 HNH endonuclease.,Zhang L, Xu D, Huang Y, Zhu X, Rui M, Wan T, Zheng X, Shen Y, Chen X, Ma K, Gong Y Sci Rep. 2017 Feb 13;7:42542. doi: 10.1038/srep42542. PMID:28211904<ref>PMID:28211904</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5h0m" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacteriophage gsve2]]
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[[Category: Geobacillus virus E2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gong, Y]]
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[[Category: Gong Y]]
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[[Category: Huang, Y C]]
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[[Category: Huang YC]]
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[[Category: Xu, D D]]
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[[Category: Xu DD]]
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[[Category: Zhang, L K]]
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[[Category: Zhang LK]]
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[[Category: Dna nicking]]
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[[Category: Hnh endonuclease]]
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[[Category: Hydrolase]]
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[[Category: Thermophilic bacteriophage]]
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Current revision

Crystal structure of deep-sea thermophilic bacteriophage GVE2 HNH endonuclease with zinc ion

PDB ID 5h0m

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