1pxw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 3: Line 3:
<StructureSection load='1pxw' size='340' side='right'caption='[[1pxw]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
<StructureSection load='1pxw' size='340' side='right'caption='[[1pxw]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pxw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pxw]] 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=1PXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXW FirstGlance]. <br>
</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=1pxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxw OCA], [https://pdbe.org/1pxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxw RCSB], [https://www.ebi.ac.uk/pdbsum/1pxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxw ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</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=1pxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxw OCA], [https://pdbe.org/1pxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxw RCSB], [https://www.ebi.ac.uk/pdbsum/1pxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RL7A_PYRAB RL7A_PYRAB]] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.  
[https://www.uniprot.org/uniprot/RL7A_PYRAB RL7A_PYRAB] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 19:
</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=1pxw ConSurf].
</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=1pxw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The L7Ae sRNP core protein from Pyrococcus abyssii was crystallized using the sitting-drop vapour-diffusion method. Crystals were obtained in the presence of MgCl(2), PEG 2000 MME and acetate buffer at pH 4.0. A native data set has been collected at 2.9 A resolution using a rotating-anode generator at room temperature. Crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 70.7, b = 112.9, c = 34.8 A. There are two monomers of MW 14 200 Da per asymmetric unit and the packing density V(M) is 2.45 A(3) Da(-1). A molecular-replacement analysis gave solutions for the rotation and translation functions.
Purification, crystallization and preliminary X-ray diffraction data of L7Ae sRNP core protein from Pyrococcus abyssii.,Charron C, Manival X, Charpentier B, Branlant C, Aubry A Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):122-4. Epub 2003, Dec 18. PMID:14684904<ref>PMID:14684904</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pxw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]]
*[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrococcus abyssi erauso et al. 1993]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aubry, A]]
[[Category: Pyrococcus abyssi]]
[[Category: Branlant, C]]
[[Category: Aubry A]]
[[Category: Charpentier, B]]
[[Category: Branlant C]]
[[Category: Charron, C]]
[[Category: Charpentier B]]
[[Category: Manival, X]]
[[Category: Charron C]]
[[Category: Ribosome]]
[[Category: Manival X]]