2e6l: Difference between revisions

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[[Image:2e6l.jpg|left|200px]]


{{Structure
==structure of mouse WRN exonuclease domain==
|PDB= 2e6l |SIZE=350|CAPTION= <scene name='initialview01'>2e6l</scene>, resolution 2.20&Aring;
<StructureSection load='2e6l' size='340' side='right'caption='[[2e6l]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[2e6l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E6L FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE= Wrn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e6l OCA], [https://pdbe.org/2e6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e6l RCSB], [https://www.ebi.ac.uk/pdbsum/2e6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e6l ProSAT]</span></td></tr>
|RELATEDENTRY=[[2e6m|2E6M]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e6l OCA], [http://www.ebi.ac.uk/pdbsum/2e6l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e6l RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/WRN_MOUSE WRN_MOUSE] Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity).<ref>PMID:10757812</ref> <ref>PMID:17229737</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/e6/2e6l_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=2e6l ConSurf].
<div style="clear:both"></div>


'''structure of mouse WRN exonuclease domain'''
==See Also==
 
*[[Helicase 3D structures|Helicase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2E6L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E6L OCA].
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Cho Y]]
[[Category: Cho, Y.]]
[[Category: Choi JM]]
[[Category: Choi, J M.]]
[[Category: zn-protein complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:44:30 2008''

Latest revision as of 16:49, 13 March 2024

structure of mouse WRN exonuclease domainstructure of mouse WRN exonuclease domain

Structural highlights

2e6l is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

WRN_MOUSE Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity).[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. ↑ Lombard DB, Beard C, Johnson B, Marciniak RA, Dausman J, Bronson R, Buhlmann JE, Lipman R, Curry R, Sharpe A, Jaenisch R, Guarente L. Mutations in the WRN gene in mice accelerate mortality in a p53-null background. Mol Cell Biol. 2000 May;20(9):3286-91. PMID:10757812
  2. ↑ Choi JM, Kang SY, Bae WJ, Jin KS, Ree M, Cho Y. Probing the roles of active site residues in the 3'-5' exonuclease of the Werner syndrome protein. J Biol Chem. 2007 Mar 30;282(13):9941-51. Epub 2007 Jan 16. PMID:17229737 doi:10.1074/jbc.M609657200

2e6l, resolution 2.20Å

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