5dqo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (21:55, 28 June 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of Y347F mutant of human primase p58 iron-sulfur cluster domain==
==Crystal structure of Y347F mutant of human primase p58 iron-sulfur cluster domain==
-
<StructureSection load='5dqo' size='340' side='right' caption='[[5dqo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+
<StructureSection load='5dqo' size='340' side='right'caption='[[5dqo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5dqo]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DQO FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5dqo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DQO FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.3&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l9q|3l9q]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=5dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dqo OCA], [http://pdbe.org/5dqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dqo RCSB], [http://www.ebi.ac.uk/pdbsum/5dqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dqo ProSAT]</span></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=5dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dqo OCA], [https://pdbe.org/5dqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dqo RCSB], [https://www.ebi.ac.uk/pdbsum/5dqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dqo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PRI2_HUMAN PRI2_HUMAN]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
+
[https://www.uniprot.org/uniprot/PRI2_HUMAN PRI2_HUMAN] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
DNA charge transport chemistry offers a means of long-range, rapid redox signaling. We demonstrate that the [4Fe4S] cluster in human DNA primase can make use of this chemistry to coordinate the first steps of DNA synthesis. Using DNA electrochemistry, we found that a change in oxidation state of the [4Fe4S] cluster acts as a switch for DNA binding. Single-atom mutations that inhibit this charge transfer hinder primase initiation without affecting primase structure or polymerization. Generating a single base mismatch in the growing primer duplex, which attenuates DNA charge transport, inhibits primer truncation. Thus, redox signaling by [4Fe4S] clusters using DNA charge transport regulates primase binding to DNA and illustrates chemistry that may efficiently drive substrate handoff between polymerases during DNA replication.
 +
 
 +
The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport.,O'Brien E, Holt ME, Thompson MK, Salay LE, Ehlinger AC, Chazin WJ, Barton JK Science. 2017 Feb 24;355(6327). pii: eaag1789. doi: 10.1126/science.aag1789. PMID:28232525<ref>PMID:28232525</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5dqo" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Chazin, W J]]
+
[[Category: Homo sapiens]]
-
[[Category: Salay, L E]]
+
[[Category: Large Structures]]
-
[[Category: Thompson, M K]]
+
[[Category: Chazin WJ]]
-
[[Category: Dna priming]]
+
[[Category: Salay LE]]
-
[[Category: Iron-sulfur cluster]]
+
[[Category: Thompson MK]]
-
[[Category: Replication]]
+

Current revision

Crystal structure of Y347F mutant of human primase p58 iron-sulfur cluster domain

PDB ID 5dqo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools