1j23

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<StructureSection load='1j23' size='340' side='right'caption='[[1j23]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='1j23' size='340' side='right'caption='[[1j23]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1j23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J23 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1j23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J23 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j22|1j22]], [[1j24|1j24]], [[1j25|1j25]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</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=1j23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j23 OCA], [https://pdbe.org/1j23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j23 RCSB], [https://www.ebi.ac.uk/pdbsum/1j23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j23 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=1j23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j23 OCA], [https://pdbe.org/1j23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j23 RCSB], [https://www.ebi.ac.uk/pdbsum/1j23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j23 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8TZH8_PYRFU Q8TZH8_PYRFU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1j23 ConSurf].
</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=1j23 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. Here, we report the domain organization of an archaeal homolog (Hef) of this family and the X-ray crystal structure of the middle domain, with the nuclease activity. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases, including the correspondence of the GDX(n)ERKX(3)D signature motif in Hef to the PDX(n)(E/D)XK motif in restriction enzymes. This structural study also suggests that the XPF/Rad1/Mus81/ERCC1 proteins form a dimer through each interface of the nuclease domain and the helix-hairpin-helix domain. Simultaneous disruptions of both interfaces result in their dissociation into separate monomers, with strikingly reduced endonuclease activities.
 
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X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: similarity between its endonuclease domain and restriction enzymes.,Nishino T, Komori K, Ishino Y, Morikawa K Structure. 2003 Apr;11(4):445-57. PMID:12679022<ref>PMID:12679022</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1j23" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pyrfu]]
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[[Category: Pyrococcus furiosus DSM 3638]]
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[[Category: Ishino, Y]]
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[[Category: Ishino Y]]
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[[Category: Komori, K]]
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[[Category: Komori K]]
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[[Category: Morikawa, K]]
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[[Category: Morikawa K]]
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[[Category: Nishino, T]]
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[[Category: Nishino T]]
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[[Category: Hydrolase]]
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[[Category: Structure-specific endonuclease]]
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Current revision

Crystal structure of archaeal XPF/Mus81 homolog, Hef from Pyrococcus furiosus, nuclease domain

PDB ID 1j23

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