This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1qhk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Current revision (23:48, 27 December 2023) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[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 />
 
-
==Overview==
+
==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, 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.
+
<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.
-
==About this Structure==
+
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>
-
1QHK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QHK OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10448044 10448044]
+
</div>
-
[[Category: Ribonuclease H]]
+
<div class="pdbe-citations 1qhk" style="background-color:#fffaf0;"></div>
-
[[Category: Saccharomyces cerevisiae]]
+
-
[[Category: Single protein]]
+
-
[[Category: Bycroft, M.]]
+
-
[[Category: Evans, S.P.]]
+
-
[[Category: ribonuclease hi n-terminal domain]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:42:24 2007''
+
==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

PDB ID 1qhk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools