6n9v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "6n9v" [edit=sysop:move=sysop])
Current revision (05:28, 21 November 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6n9v is ON HOLD
+
==Structure of bacteriophage T7 lagging-strand DNA polymerase (D5A/E7A) and gp4 (helicase/primase) bound to DNA including RNA/DNA hybrid, and an incoming dTTP (LagS1)==
 +
<SX load='6n9v' size='340' side='right' viewer='molstar' caption='[[6n9v]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6n9v]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T7 Escherichia phage T7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N9V FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6n9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n9v OCA], [https://pdbe.org/6n9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n9v RCSB], [https://www.ebi.ac.uk/pdbsum/6n9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n9v ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HELIC_BPT7 HELIC_BPT7] ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination (PubMed:21606333, PubMed:22977246, PubMed:32009150). The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis (PubMed:21606333, PubMed:22977246, PubMed:32009150). ATP or dTTP hydrolysis propels each helicase domain to translocate 2 nt per step sequentially along DNA (PubMed:17604719, PubMed:30679383). Mediates strand transfer when a joint molecule is available and participates in recombinational DNA repair through its role in strand exchange (PubMed:8617248, PubMed:9096333). Primase activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the lagging strand that the polymerase elongates using dNTPs and providing the primase is still present (PubMed:6454135, PubMed:9139692).[HAMAP-Rule:MF_04154]<ref>PMID:17604719</ref> <ref>PMID:21606333</ref> <ref>PMID:22977246</ref> <ref>PMID:30679383</ref> <ref>PMID:32009150</ref> <ref>PMID:6454135</ref> <ref>PMID:8617248</ref> <ref>PMID:9096333</ref> <ref>PMID:9139692</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Visualization in atomic detail of the replisome that performs concerted leading- and lagging-DNA strand synthesis at a replication fork has not been reported. Using bacteriophage T7 as a model system, we determined cryo-electron microscopy structures up to 3.2-angstroms resolution of helicase translocating along DNA and of helicase-polymerase-primase complexes engaging in synthesis of both DNA strands. Each domain of the spiral-shaped hexameric helicase translocates sequentially hand-over-hand along a single-stranded DNA coil, akin to the way AAA+ ATPases (adenosine triphosphatases) unfold peptides. Two lagging-strand polymerases are attached to the primase, ready for Okazaki fragment synthesis in tandem. A beta hairpin from the leading-strand polymerase separates two parental DNA strands into a T-shaped fork, thus enabling the closely coupled helicase to advance perpendicular to the downstream DNA duplex. These structures reveal the molecular organization and operating principles of a replisome.
-
Authors: Gao, Y., Fox, T., Val, N., Yang, W.
+
Structures and operating principles of the replisome.,Gao Y, Cui Y, Fox T, Lin S, Wang H, de Val N, Zhou ZH, Yang W Science. 2019 Feb 22;363(6429). pii: science.aav7003. doi:, 10.1126/science.aav7003. Epub 2019 Jan 24. PMID:30679383<ref>PMID:30679383</ref>
-
Description: Structure of gp5 DNA polymerase binding to A and F subunits of gp4 primase-helicase hexamer complexed with trx, RNA/DNA hybrid, and incoming dTTP (LagS1)
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Gao, Y]]
+
<div class="pdbe-citations 6n9v" style="background-color:#fffaf0;"></div>
-
[[Category: Val, N]]
+
 
-
[[Category: Fox, T]]
+
==See Also==
-
[[Category: Yang, W]]
+
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 +
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</SX>
 +
[[Category: Escherichia phage T7]]
 +
[[Category: Large Structures]]
 +
[[Category: Fox T]]
 +
[[Category: Gao Y]]
 +
[[Category: Val N]]
 +
[[Category: Yang W]]

Current revision

Structure of bacteriophage T7 lagging-strand DNA polymerase (D5A/E7A) and gp4 (helicase/primase) bound to DNA including RNA/DNA hybrid, and an incoming dTTP (LagS1)

6n9v, resolution 4.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6n9v"
Personal tools