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1qhk
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1qhk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qhk" /> '''N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIA...) |
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| - | [[Image:1qhk.jpg|left|200px]]<br /><applet load="1qhk" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1qhk" /> | ||
| - | '''N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9'''<br /> | ||
| - | == | + | ==N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9== |
| - | In addition to the conserved and well-defined RNase H domain, eukaryotic | + | <StructureSection load='1qhk' size='340' side='right'caption='[[1qhk]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1qhk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QHK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1qhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qhk OCA], [https://pdbe.org/1qhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qhk RCSB], [https://www.ebi.ac.uk/pdbsum/1qhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qhk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RNH1_YEAST RNH1_YEAST] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qh/1qhk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1qhk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In addition to the conserved and well-defined RNase H domain, eukaryotic RNases HI possess either one or two copies of a small N-terminal domain. The solution structure of one of the N-terminal domains from Saccharomyces cerevisiae RNase HI, determined using NMR spectroscopy, is presented. The 46 residue motif comprises a three-stranded antiparallel beta-sheet and two short alpha-helices which pack onto opposite faces of the beta-sheet. Conserved residues involved in packing the alpha-helices onto the beta-sheet form the hydrophobic core of the domain. Three highly conserved and solvent exposed residues are implicated in RNA binding, W22, K38 and K39. The beta-beta-alpha-beta-alpha topology of the domain differs from the structures of known RNA binding domains such as the double-stranded RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP motif. However, structural similarities exist between this domain and the N-terminal domain of ribosomal protein L9 which binds to 23 S ribosomal RNA. | ||
| - | + | NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9.,Evans SP, Bycroft M J Mol Biol. 1999 Aug 20;291(3):661-9. PMID:10448044<ref>PMID:10448044</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1qhk" style="background-color:#fffaf0;"></div> | |
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| - | + | ||
| - | + | ==See Also== | |
| + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Bycroft M]] | ||
| + | [[Category: Evans SP]] | ||
Current revision
N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9
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