View source for 3rjz


==X-ray crystal structure of the putative n-type atp pyrophosphatase from pyrococcus furiosus, the northeast structural genomics target pfr23==
<StructureSection load='3rjz' size='340' side='right'caption='[[3rjz]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rjz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrfu Pyrfu]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ru8 1ru8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RJZ FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rk0|3rk0]], [[3rk1|3rk1]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF0828 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=3rjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rjz OCA], [https://pdbe.org/3rjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rjz RCSB], [https://www.ebi.ac.uk/pdbsum/3rjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rjz ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ATP pyrophosphatases (ATP PPases) are widely distributed in archaea and eukaryotes. They share an HUP domain at the N-terminus with a conserved PP-motif that interacts with the phosphates of ATP. The PF0828 protein from Pyrococcus furiosus is a member of the ATP PPase superfamily and it also has a 100-residue C-terminal extension that contains a strictly conserved EGG(E/D)xE(T/S) motif, which has been named the EGT-motif. Here, crystal structures of PF0828 alone and in complex with ATP or AMP are reported. The HUP domain contains a central five-stranded beta-sheet that is surrounded by four helices, as in other related structures. The C-terminal extension forms a separate domain, named the EGT domain, which makes tight interactions with the HUP domain, bringing the EGT-motif near to the PP-motif and defining the putative active site of PF0828. Both motifs interact with the phosphate groups of ATP. A loop in the HUP domain undergoes a large conformational change to recognize the adenine base of ATP. In solution and in the crystal PF0828 is a dimer formed by the side-by-side arrangement of the HUP domains of the two monomers. The putative active site is located far from the dimer interface.

A large conformational change in the putative ATP pyrophosphatase PF0828 induced by ATP binding.,Forouhar F, Saadat N, Hussain M, Seetharaman J, Lee I, Janjua H, Xiao R, Shastry R, Acton TB, Montelione GT, Tong L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt, 11):1323-7. Epub 2011 Oct 25. PMID:22102225<ref>PMID:22102225</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3rjz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrfu]]
[[Category: Acton, T B]]
[[Category: Forouhar, F]]
[[Category: Hunt, J]]
[[Category: Lee, I]]
[[Category: Montelione, G T]]
[[Category: Structural genomic]]
[[Category: Tong, L]]
[[Category: Xiao, R]]
[[Category: Alpha-beta protein]]
[[Category: Hydrolase]]
[[Category: N-type atp pyrophosphatase]]
[[Category: Nesg]]
[[Category: Psi-biology]]