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.


4wkj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:32, 27 September 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystallographic Structure of a Dodecameric RNA-DNA Hybrid==
==Crystallographic Structure of a Dodecameric RNA-DNA Hybrid==
-
<StructureSection load='4wkj' size='340' side='right' caption='[[4wkj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+
<StructureSection load='4wkj' size='340' side='right'caption='[[4wkj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4wkj]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WKJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WKJ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4wkj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WKJ FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.8&#8491;</td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wkj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wkj RCSB], [http://www.ebi.ac.uk/pdbsum/4wkj PDBsum]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4wkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wkj OCA], [https://pdbe.org/4wkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wkj RCSB], [https://www.ebi.ac.uk/pdbsum/4wkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wkj ProSAT]</span></td></tr>
</table>
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
RNA-DNA hybrids play essential roles in a variety of biological processes, including DNA replication, transcription, and viral integration. Ribonucleotides incorporated within DNA are hydrolyzed by RNase H enzymes in a removal process that is necessary for maintaining genomic stability. In order to understand the structural determinants involved in recognition of a hybrid substrate by RNase H we have determined the crystal structure of a dodecameric non-polypurine/polypyrimidine tract RNA-DNA duplex. A comparison to the same sequence bound to RNase H, reveals structural changes to the duplex that include widening of the major groove to 12.5 A from 4.2 A and decreasing the degree of bending along the axis which may play a crucial role in the ribonucleotide recognition and cleavage mechanism within RNase H. This structure allows a direct comparison to be made about the conformational changes induced in RNA-DNA hybrids upon binding to RNase H and may provide insight into how dysfunction in the endonuclease causes disease.
 +
 +
Crystal structure of RNA-DNA duplex provides insight into conformational changes induced by RNase H binding.,Davis RR, Shaban NM, Perrino FW, Hollis T Cell Cycle. 2015 Feb 16;14(4):668-73. doi: 10.4161/15384101.2014.994996. PMID:25664393<ref>PMID:25664393</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4wkj" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Davis, R R.]]
+
[[Category: Escherichia coli]]
-
[[Category: Hollis, T.]]
+
[[Category: Large Structures]]
-
[[Category: Perrino, F W.]]
+
[[Category: Davis RR]]
-
[[Category: Shaban, N M.]]
+
[[Category: Hollis T]]
-
[[Category: Dna]]
+
[[Category: Perrino FW]]
-
[[Category: Duplex]]
+
[[Category: Shaban NM]]
-
[[Category: Hybrid]]
+
-
[[Category: Rna]]
+
-
[[Category: Rna-dna complex]]
+

Current revision

Crystallographic Structure of a Dodecameric RNA-DNA Hybrid

PDB ID 4wkj

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools