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2mjp

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[[Image:2mjp.gif|left|200px]]
 
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{{Structure
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==STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226==
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|PDB= 2mjp |SIZE=350|CAPTION= <scene name='initialview01'>2mjp</scene>, resolution 2.2&Aring;
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<StructureSection load='2mjp' size='340' side='right'caption='[[2mjp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<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>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00515 HAM1]</span>
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<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>
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|RELATEDENTRY=[[1b78|1B78]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjp OCA], [http://www.ebi.ac.uk/pdbsum/2mjp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2mjp RCSB]</span>
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== Function ==
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}}
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mj/2mjp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mjp" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2MJP is a [[Single protein]] structure of 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=2MJP OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10404228 10404228]
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[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
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[[Category: Single protein]]
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[[Category: Cho Y]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
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[[Category: Chung JH]]
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[[Category: Cho, Y.]]
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[[Category: Han YS]]
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[[Category: Chung, J H.]]
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[[Category: Hwang KY]]
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[[Category: Han, Y S.]]
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[[Category: Kim SH]]
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[[Category: Hwang, K Y.]]
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[[Category: Kim, S H.]]
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[[Category: berkeley structural genomics center]]
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[[Category: bsgc structure funded by nih]]
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[[Category: hyperthermal protein]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: pyrophosphatase]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:04:21 2008''
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Current revision

STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226

PDB ID 2mjp

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