4nsp: Difference between revisions
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nsp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nsp RCSB], [http://www.ebi.ac.uk/pdbsum/4nsp PDBsum]</span></td></tr> | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nsp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nsp RCSB], [http://www.ebi.ac.uk/pdbsum/4nsp PDBsum]</span></td></tr> | ||
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<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 6-aminopurine ring of adenosine (A) can be deaminated to form the 6-oxopurine of inosine (I). Endonuclease Vs (EndoVs) are inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine. EndoV proteins are highly conserved in all domains of life, but the bacterial and human enzymes seem to display distinct substrate preferences. While the bacterial enzymes exhibit high cleavage efficiency on various nucleic acid substrates, human EndoV (hEndoV) is most active towards ssRNA but is much less active towards other substrates. However, the structural basis of substrate recognition by hEndoV is not well understood. In this study, the 2.3 A resolution crystal structure of hEndoV was determined and its unusual RNA-cleaving properties were investigated. The enzyme preserves the general `RNase H-like' structure, especially in the wedge motif, the metal-binding site and the hypoxanthine-binding pocket. hEndoV also features several extra insertions and a characteristic four-cysteine motif, in which Cys227 and Cys228, two cysteines that are highly conserved in higher eukaryotes, play important roles in catalysis. The structure presented here helps in understanding the substrate preference of hEndoV catalysis. | |||
Structure of human endonuclease V as an inosine-specific ribonuclease.,Zhang Z, Hao Z, Wang Z, Li Q, Xie W Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2286-94. doi:, 10.1107/S139900471401356X. Epub 2014 Aug 29. PMID:25195743<ref>PMID:25195743</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 10:01, 24 September 2014
Crystal structure of human ENDOVCrystal structure of human ENDOV
Structural highlights
Publication Abstract from PubMedThe 6-aminopurine ring of adenosine (A) can be deaminated to form the 6-oxopurine of inosine (I). Endonuclease Vs (EndoVs) are inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine. EndoV proteins are highly conserved in all domains of life, but the bacterial and human enzymes seem to display distinct substrate preferences. While the bacterial enzymes exhibit high cleavage efficiency on various nucleic acid substrates, human EndoV (hEndoV) is most active towards ssRNA but is much less active towards other substrates. However, the structural basis of substrate recognition by hEndoV is not well understood. In this study, the 2.3 A resolution crystal structure of hEndoV was determined and its unusual RNA-cleaving properties were investigated. The enzyme preserves the general `RNase H-like' structure, especially in the wedge motif, the metal-binding site and the hypoxanthine-binding pocket. hEndoV also features several extra insertions and a characteristic four-cysteine motif, in which Cys227 and Cys228, two cysteines that are highly conserved in higher eukaryotes, play important roles in catalysis. The structure presented here helps in understanding the substrate preference of hEndoV catalysis. Structure of human endonuclease V as an inosine-specific ribonuclease.,Zhang Z, Hao Z, Wang Z, Li Q, Xie W Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2286-94. doi:, 10.1107/S139900471401356X. Epub 2014 Aug 29. PMID:25195743[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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