7y56
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of NS1 nuclease domain in P41212 space group== | |
| + | <StructureSection load='7y56' size='340' side='right'caption='[[7y56]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7y56]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_parvovirus_B19 Human parvovirus B19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y56 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]] 1.752Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7y56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y56 OCA], [https://pdbe.org/7y56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y56 RCSB], [https://www.ebi.ac.uk/pdbsum/7y56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y56 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q75U85_PAVHB Q75U85_PAVHB] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Infection of human parvovirus B19 (B19V) can cause a variety of diseases, such as hydrops fetalis, erythema infectiosum in children and acute arthropathy in women. Although B19V infection mainly occurs during childhood, about 50 % of adults are still susceptible to B19V infection. As the major replication protein of B19V, deletion of NS1 completely abolishes the infectivity of the virus. The nuclease domain of NS1 (NS1_Nuc) is responsible for DNA Ori binding and nicking that is critical for B19V viral DNA replication. NS1 has various variants, the structure and function for the majority of the variants are poorly studied. Here, we report two high-resolution crystal structures of NS1_Nuc, revealed the detailed conformations of many key residues. Structural comparison indicates that these residues are important for ssDNA or dsDNA binding by NS1. NS1 belongs to the HUH-endonuclease superfamily and it shares conserved ssDNA cleavage mechanism with other HUH-endonuclease members. However, our structural analyses, mutagenesis and in vitro assay results all suggested that NS1_Nuc utilizes one unique model in ssDNA binding. | ||
| - | + | Structures and implications of the nuclease domain of human parvovirus B19 NS1 protein.,Zhang Y, Shao Z, Gao Y, Fan B, Yang J, Chen X, Zhao X, Shao Q, Zhang W, Cao C, Liu H, Gan J Comput Struct Biotechnol J. 2022 Aug 27;20:4645-4655. doi: , 10.1016/j.csbj.2022.08.047. eCollection 2022. PMID:36090819<ref>PMID:36090819</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7y56" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human parvovirus B19]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gan JH]] | ||
| + | [[Category: Zhang XY]] | ||
Current revision
Crystal structure of NS1 nuclease domain in P41212 space group
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