1h64

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(New page: 200px<br /><applet load="1h64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h64, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1h64.gif|left|200px]]<br /><applet load="1h64" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h64, resolution 1.9&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE SM-RELATED PROTEIN OF P. ABYSSI THE BIOLOGICAL UNIT IS A HEPTAMER'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE SM-RELATED PROTEIN OF P. ABYSSI: THE BIOLOGICAL UNIT IS A HEPTAMER==
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The Sm proteins are conserved in all three domains of life and are always, associated with U-rich RNA sequences. Their proposed function is to, mediate RNA-RNA interactions. We present here the crystal structures of, Pyrococcus abyssi Sm protein (PA-Sm1) and its complex with a uridine, heptamer. The overall structure of the protein complex, a heptameric ring, with a central cavity, is similar to that proposed for the eukaryotic Sm, core complex and found for other archaeal Sm proteins. RNA molecules bind, to the protein at two different sites. They interact specifically inside, the ring with three highly conserved residues, defining the, uridine-binding pocket. In addition, nucleotides also interact on the, surface formed by the N-terminal alpha-helix as well as a conserved, aromatic residue in beta-strand 2 of the PA-Sm1 protein. The mutation of, this conserved aromatic residue shows the importance of this second site, for the discrimination between RNA sequences. Given the high structural, homology between archaeal and eukaryotic Sm proteins, the PA-Sm1.RNA, complex provides a model for how the small nuclear RNA contacts the Sm, proteins in the Sm core. In addition, it suggests how Sm proteins might, exert their function as modulators of RNA-RNA interactions.
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<StructureSection load='1h64' size='340' side='right'caption='[[1h64]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h64]] is a 28 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=1H64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H64 FirstGlance]. <br>
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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]] 1.9&#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=1h64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h64 OCA], [https://pdbe.org/1h64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h64 RCSB], [https://www.ebi.ac.uk/pdbsum/1h64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h64 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RUXX_PYRAB RUXX_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/h6/1h64_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=1h64 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1H64 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H64 OCA].
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*[[Sm-like protein 3D structures|Sm-like protein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in archaea and eukarya., Thore S, Mayer C, Sauter C, Weeks S, Suck D, J Biol Chem. 2003 Jan 10;278(2):1239-47. Epub 2002 Oct 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12409299 12409299]
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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: Mayer C]]
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[[Category: Mayer, C.]]
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[[Category: Suck D]]
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[[Category: Suck, D.]]
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[[Category: Weeks S]]
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[[Category: Weeks, S.]]
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[[Category: sm fold]]
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[[Category: sm-like protein]]
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[[Category: snrnp core]]
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[[Category: spliceosome]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:25:54 2007''
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Current revision

CRYSTAL STRUCTURE OF THE SM-RELATED PROTEIN OF P. ABYSSI: THE BIOLOGICAL UNIT IS A HEPTAMER

PDB ID 1h64

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