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2p38

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(New page: 200px<br /><applet load="2p38" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p38, resolution 1.80&Aring;" /> '''Crystal Structure of...)
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[[Image:2p38.jpg|left|200px]]<br /><applet load="2p38" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2p38, resolution 1.80&Aring;" />
 
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'''Crystal Structure of Pyrococcus Abyssi Protein Homologue of Saccharomyces Cerevisiae NIP7P'''<br />
 
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==Overview==
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==Crystal Structure of Pyrococcus Abyssi Protein Homologue of Saccharomyces Cerevisiae NIP7P==
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The conserved protein Nip7 is involved in ribosome biogenesis, being, required for proper 27S pre-rRNA processing and 60S ribosome subunit, assembly in Saccharomyces cerevisiae. Yeast Nip7p interacts with nucleolar, proteins and with the exosome subunit Rrp43p, but its molecular function, remains to be determined. Solution of the Pyrococcus abyssi Nip7 (PaNip7), crystal structure revealed a monomeric protein composed by two alpha-beta, domains. The N-terminal domain is formed by a five-stranded antiparallel, beta-sheet surrounded by three alpha-helices and a 310 helix while the, C-terminal, a mixed beta-sheet domain composed by strands beta8 to beta12, one alpha-helix, and a 310 helix, corresponds to the conserved PUA domain, (after Pseudo-Uridine synthases and Archaeosine-specific, transglycosylases). By combining structural analyses and RNA interaction, assays, we assessed the ability of both yeast and archaeal Nip7, orthologues to interact with RNA. Structural alignment of the PaNip7 PUA, domain with the RNA-interacting surface of the ArcTGT (archaeosine, tRNA-guanine transglycosylase) PUA domain indicated that in the archaeal, PUA domain positively charged residues (R151, R152, K155, and K158) are, involved in RNA interaction. However, equivalent positions are occupied by, mostly hydrophobic residues (A/G160, I161, F164, and A167) in eukaryotic, Nip7 orthologues. Both proteins can bind specifically to polyuridine, and, RNA interaction requires specific residues of the PUA domain as determined, by site-directed mutagenesis. This work provides experimental verification, that the PUA domain mediates Nip7 interaction with RNA and reveals that, the preference for interaction with polyuridine sequences is conserved in, Archaea and eukaryotic Nip7 proteins.
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<StructureSection load='2p38' size='340' side='right'caption='[[2p38]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2p38]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P38 FirstGlance]. <br>
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2P38 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P38 OCA].
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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]] 1.8&#8491;</td></tr>
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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=2p38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p38 OCA], [https://pdbe.org/2p38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p38 RCSB], [https://www.ebi.ac.uk/pdbsum/2p38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p38 ProSAT]</span></td></tr>
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==Reference==
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</table>
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Structural insights into the interaction of the Nip7 PUA domain with polyuridine RNA., Coltri PP, Guimaraes BG, Granato DC, Luz JS, Teixeira EC, Oliveira CC, Zanchin NI, Biochemistry. 2007 Dec 11;46(49):14177-87. Epub 2007 Nov 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18001138 18001138]
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== Function ==
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[https://www.uniprot.org/uniprot/Q9V219_PYRAB Q9V219_PYRAB]
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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/p3/2p38_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=2p38 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pyrococcus abyssi]]
[[Category: Pyrococcus abyssi]]
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[[Category: Single protein]]
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[[Category: Coltri PP]]
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[[Category: Coltri, P.P.]]
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[[Category: Guimaraes BG]]
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[[Category: Guimaraes, B.G.]]
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[[Category: Oliveira CC]]
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[[Category: Oliveira, C.C.]]
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[[Category: Zanchin NIT]]
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[[Category: Zanchin, N.I.T.]]
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[[Category: biosynthetic protein]]
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[[Category: pua domain]]
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[[Category: two alpha/beta domains]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:06:47 2008''
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Current revision

Crystal Structure of Pyrococcus Abyssi Protein Homologue of Saccharomyces Cerevisiae NIP7P

PDB ID 2p38

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