1j25
From Proteopedia
(New page: 200px<br /><applet load="1j25" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j25, resolution 1.78Å" /> '''Crystal structure of...) |
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| - | [[Image:1j25.jpg|left|200px]]<br /><applet load="1j25" size=" | + | [[Image:1j25.jpg|left|200px]]<br /><applet load="1j25" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j25, resolution 1.78Å" /> | caption="1j25, resolution 1.78Å" /> | ||
'''Crystal structure of archaeal XPF/Mus81 homolog, Hef from Pyrococcus furiosus, nuclease domain, Mn cocrystal'''<br /> | '''Crystal structure of archaeal XPF/Mus81 homolog, Hef from Pyrococcus furiosus, nuclease domain, Mn cocrystal'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1J25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_dsm_3638 Pyrococcus furiosus dsm 3638] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1J25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_dsm_3638 Pyrococcus furiosus dsm 3638] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J25 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structure-specific endonuclease]] | [[Category: structure-specific endonuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:09 2008'' |
Revision as of 11:18, 21 February 2008
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Crystal structure of archaeal XPF/Mus81 homolog, Hef from Pyrococcus furiosus, nuclease domain, Mn cocrystal
Overview
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.
About this Structure
1J25 is a Single protein structure of sequence from Pyrococcus furiosus dsm 3638 with as ligand. Full crystallographic information is available from OCA.
Reference
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
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