NudT16

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<StructureSection load='6B09' size='350' side='right' caption='Crystal structure of HsNUDT16 in complex with diADPR, one monomer is shown in cyan with amino acids 4-17 in blue, the other monomer is shown in purple and has residues 3-17 colored in pink. (PDB entry [[6B09]])' scene='84/849734/Nudt16/5'>
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<StructureSection load='6B09' size='350' side='right' caption='Crystal structure of HsNUDT16 in complex with diADPR, one monomer is shown in cyan with amino acids 4-17 in blue, the other monomer is shown in purple and has residues 3-17 colored in pink. (PDB entry [[6b09]])' scene='84/849734/Nudt16/5'>
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==Introduction==
==Introduction==
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NudT16 is an archetypical member of the Nudix superfamily of hydrolases. Nudix hydrolases have in common a stretch of 23 amino acids called the Nudix signature sequence which is the binding site for the metal involved in diphosphate hydrolysis. Nudix hydrolases prefer substrates of the form NUcleoside, DIphosphate and X, hence their name NUDIX. Examples of such substrates are ATP where X is PPI, ADPribose where X is phospho-ribose or m7GTP-RNA where X is phospho-RNA. Their catalytic activity breakshydrolyze a phosphorus-oxygen bond resulting in a nucleoside monophosphate (NMP) and a phosphate linked to moiety X. While NudT16 was initially described as a nuclear RNA and cytoplasmic mRNA decapping enzyme, further studies have shown that it also effectively hydrolyzes inosine diphosphate (IDP) and its hazardous deoxyribose cognate (dIDP) into inosine monophosphate (IMP) and deoxy inosine monophosphate (dIMP), respectively <ref>PMID: 26121039</ref>. NudT16 was shown to hydrolyze ADPribose and polyADPr <ref>PMID: 30976021</ref>. Physiologically, NudT16 has been shown to regulate levels of 53BP1, an adaptor protein that recruits other proteins to the site of a DNA breakage, through hydrolytic removal of ADP-ribose (ADPr) from Poly-ADP-ribosylated 53BP1 <ref>PMID: 31911551</ref>.
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'''NudT16''' is an archetypical member of the Nudix superfamily of hydrolases. [[Nudix hydrolase]] enzymes have in common a stretch of 23 amino acids called the Nudix signature sequence which is the binding site for the metal involved in diphosphate hydrolysis. Nudix hydrolases prefer substrates of the form '''NU'''cleoside, '''DI'''phosphate and variable motif'''X''', hence their name NUDIX. Examples of such substrates are ATP where X is PPI, ADP-ribose where X is phospho-ribose or m7GTP-RNA where X is phospho-RNA. Their catalytic activity is to hydrolyze a phosphorus-oxygen bond resulting in a nucleoside monophosphate (NMP) and a phosphate linked to moiety X.
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While NudT16 was initially described as a nuclear RNA and cytoplasmic mRNA decapping enzyme, further studies have shown that it also effectively hydrolyzes inosine diphosphate (IDP) and its hazardous deoxyribose cognate (dIDP) into inosine monophosphate (IMP) and deoxy inosine monophosphate (dIMP), respectively <ref>PMID: 26121039</ref>. NudT16 has also been shown to hydrolyze ADP-ribose (ADPr) and Poly-ADP-ribose (polyADPr) <ref>PMID: 30976021</ref>. Physiologically, NudT16 has been shown to regulate levels of 53BP1, an adaptor protein that recruits other proteins to the site of a DNA breakage, through hydrolytic removal of ADPr from Poly-ADP-ribosylated 53BP1 <ref>PMID: 31911551</ref>.
==Structure==
==Structure==
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Iyama et. al. determined that NudT16 is a (Deoxy)inosine diphosphatase and that the loss of this protein is followed by increased accumulation of single-strand breaks in DNA, reduced proliferation, and increased cell arrest. They also found increased levels of inosine in RNA, which informed the conclusion that HsNudT16 functions in the nucleus to protect the cell from ITP and its detrimental effects <ref>PMID:20385596</ref> .
Iyama et. al. determined that NudT16 is a (Deoxy)inosine diphosphatase and that the loss of this protein is followed by increased accumulation of single-strand breaks in DNA, reduced proliferation, and increased cell arrest. They also found increased levels of inosine in RNA, which informed the conclusion that HsNudT16 functions in the nucleus to protect the cell from ITP and its detrimental effects <ref>PMID:20385596</ref> .
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== Relevance ==
 
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== References ==
== References ==
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Current revision

Crystal structure of HsNUDT16 in complex with diADPR, one monomer is shown in cyan with amino acids 4-17 in blue, the other monomer is shown in purple and has residues 3-17 colored in pink. (PDB entry 6b09)

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Proteopedia Page Contributors and Editors (what is this?)

Hannah Campbell, Tihitina Y Aytenfisu, Michal Harel, Sandra B. Gabelli

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