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| | <StructureSection load='1b78' size='340' side='right'caption='[[1b78]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1b78' size='340' side='right'caption='[[1b78]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b78]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B78 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b78]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B78 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mjp|2mjp]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b78 OCA], [http://pdbe.org/1b78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b78 RCSB], [http://www.ebi.ac.uk/pdbsum/1b78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b78 ProSAT]</span></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=1b78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b78 OCA], [https://pdbe.org/1b78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b78 RCSB], [https://www.ebi.ac.uk/pdbsum/1b78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b78 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NTPA_METJA NTPA_METJA]] Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective monophosphate derivatives. Probably excludes non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions.<ref>PMID:10404228</ref> | + | [https://www.uniprot.org/uniprot/IXTPA_METJA IXTPA_METJA] Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP (PubMed:10404228, PubMed:11452035). Probably functions as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions (PubMed:11452035). Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than XTP, and has nearly no activity toward the canonical nucleotides ATP, CTP, and TTP, and toward 6-N-hydroxylaminopurine deoxynucleoside triphosphate (dHAPTP) (PubMed:10404228, PubMed:11452035). Displays neither endonuclease nor 3'-exonuclease activities (PubMed:11452035).<ref>PMID:10404228</ref> <ref>PMID:11452035</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Inorganic pyrophosphatase|Inorganic pyrophosphatase]] | + | *[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Methanocaldococcus jannaschii]] | | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Cho, Y]] | + | [[Category: Cho Y]] |
| - | [[Category: Chung, J H]] | + | [[Category: Chung JH]] |
| - | [[Category: Han, Y S]] | + | [[Category: Han YS]] |
| - | [[Category: Hwang, K Y]] | + | [[Category: Hwang KY]] |
| - | [[Category: Kim, S H]] | + | [[Category: Kim SH]] |
| - | [[Category: Hyperthermal protein]]
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| - | [[Category: Pyrophosphatase]]
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| - | [[Category: Structural genomic]]
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| Structural highlights
Function
IXTPA_METJA Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP (PubMed:10404228, PubMed:11452035). Probably functions as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions (PubMed:11452035). Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than XTP, and has nearly no activity toward the canonical nucleotides ATP, CTP, and TTP, and toward 6-N-hydroxylaminopurine deoxynucleoside triphosphate (dHAPTP) (PubMed:10404228, PubMed:11452035). Displays neither endonuclease nor 3'-exonuclease activities (PubMed:11452035).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Almost half of the entire set of predicted genomic products from Methanococcus jannaschii are classified as functionally unknown hypothetical proteins. We present a structure-based identification of the biochemical function of a protein with an as yet unknown function from a M. jannaschii gene, Mj0226. The crystal structure of Mj0226 protein determined at 2.2 A resolution reveals that the protein is a homodimer and each monomer folds into an elongated alpha/beta structure of a new fold family. Comparisons of Mj0226 protein with protein structures in the database, however, indicate that one part of the protein is homologous to some of the nucleotide-binding proteins. Biochemical analysis shows that Mj0226 protein is a novel nucleotide triphosphatase that can efficiently hydrolyze nonstandard nucleotides such as XTP to XMP or ITP to IMP, but not the standard nucleotides, in the presence of Mg2+ or Mn2+ ions.
Structure-based identification of a novel NTPase from Methanococcus jannaschii.,Hwang KY, Chung JH, Kim SH, Han YS, Cho Y Nat Struct Biol. 1999 Jul;6(7):691-6. PMID:10404228[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hwang KY, Chung JH, Kim SH, Han YS, Cho Y. Structure-based identification of a novel NTPase from Methanococcus jannaschii. Nat Struct Biol. 1999 Jul;6(7):691-6. PMID:10404228 doi:10.1038/10745
- ↑ Chung JH, Back JH, Park YI, Han YS. Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii. Nucleic Acids Res. 2001 Jul 15;29(14):3099-107. PMID:11452035 doi:10.1093/nar/29.14.3099
- ↑ Hwang KY, Chung JH, Kim SH, Han YS, Cho Y. Structure-based identification of a novel NTPase from Methanococcus jannaschii. Nat Struct Biol. 1999 Jul;6(7):691-6. PMID:10404228 doi:10.1038/10745
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