1skr: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1skr.png|left|200px]]


{{STRUCTURE_1skr|  PDB=1skr  |  SCENE=  }}
==T7 DNA Polymerase Complexed To DNA Primer/Template and ddATP==
 
<StructureSection load='1skr' size='340' side='right'caption='[[1skr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
===T7 DNA Polymerase Complexed To DNA Primer/Template and ddATP===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1skr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [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=1SKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SKR FirstGlance]. <br>
{{ABSTRACT_PUBMED_15235589}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DA:2,3-DIDEOXYADENOSINE-5-MONOPHOSPHATE'>2DA</scene>, <scene name='pdbligand=DAD:2,3-DIDEOXYADENOSINE-5-TRIPHOSPHATE'>DAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1skr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1skr OCA], [https://pdbe.org/1skr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1skr RCSB], [https://www.ebi.ac.uk/pdbsum/1skr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1skr ProSAT]</span></td></tr>
[[1skr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t7 Enterobacteria phage t7] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SKR OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPOL_BPT7 DPOL_BPT7] Replicates viral genomic DNA. Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.<ref>PMID:9218486</ref> <ref>PMID:21606333</ref>
== 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/sk/1skr_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=1skr ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[DNA polymerase|DNA polymerase]]
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
*[[Thioredoxin|Thioredoxin]]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015235589</ref><references group="xtra"/>
__TOC__
[[Category: DNA-directed DNA polymerase]]
</StructureSection>
[[Category: Enterobacteria phage t7]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Bdour, H M.]]
[[Category: Escherichia phage T7]]
[[Category: Doublie, S.]]
[[Category: Large Structures]]
[[Category: Dutta, S.]]
[[Category: Bdour HM]]
[[Category: Ellenberger, T.]]
[[Category: Doublie S]]
[[Category: Li, Y.]]
[[Category: Dutta S]]
[[Category: Taylor, J S.]]
[[Category: Ellenberger T]]
[[Category: Close]]
[[Category: Li Y]]
[[Category: Dna polymerase]]
[[Category: Taylor JS]]
[[Category: Open]]
[[Category: Replication]]
[[Category: Transferase-electron transport-dna complex]]
[[Category: Uv-lesion]]

Latest revision as of 11:31, 14 February 2024

T7 DNA Polymerase Complexed To DNA Primer/Template and ddATPT7 DNA Polymerase Complexed To DNA Primer/Template and ddATP

Structural highlights

1skr is a 4 chain structure with sequence from Escherichia coli and Escherichia phage T7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPOL_BPT7 Replicates viral genomic DNA. Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Notarnicola SM, Mulcahy HL, Lee J, Richardson CC. The acidic carboxyl terminus of the bacteriophage T7 gene 4 helicase/primase interacts with T7 DNA polymerase. J Biol Chem. 1997 Jul 18;272(29):18425-33. PMID:9218486
  2. Zhang H, Lee SJ, Zhu B, Tran NQ, Tabor S, Richardson CC. Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis. Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9372-7. doi:, 10.1073/pnas.1106678108. Epub 2011 May 23. PMID:21606333 doi:http://dx.doi.org/10.1073/pnas.1106678108

1skr, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA