2mjp
From Proteopedia
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| - | [[Image:2mjp.gif|left|200px]] | ||
| - | + | ==STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226== | |
| - | + | <StructureSection load='2mjp' size='340' side='right'caption='[[2mjp]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[2mjp]] 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=2MJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJP 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]] 2.2Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=2mjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjp OCA], [https://pdbe.org/2mjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mjp RCSB], [https://www.ebi.ac.uk/pdbsum/2mjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjp ProSAT], [https://www.topsan.org/Proteins/BSGC/2mjp TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| + | [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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mj/2mjp_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2mjp ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:10404228</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2mjp" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
| - | + | [[Category: Cho Y]] | |
| - | + | [[Category: Chung JH]] | |
| - | [[Category: Cho | + | [[Category: Han YS]] |
| - | [[Category: Chung | + | [[Category: Hwang KY]] |
| - | [[Category: Han | + | [[Category: Kim SH]] |
| - | [[Category: Hwang | + | |
| - | [[Category: Kim | + | |
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Current revision
STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226
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