1yd4: Difference between revisions

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[[Image:1yd4.gif|left|200px]]<br /><applet load="1yd4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1yd4.gif|left|200px]]<br /><applet load="1yd4" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1yd4, resolution 1.90Å" />

'''Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y29F bound to its catalytic divalent cation'''<br />

==Overview==

Nucleotide excision repair is a highly conserved DNA repair mechanism, present in all kingdoms of life. The incision reaction is a critical step, for damage removal and is accomplished by the UvrC protein in eubacteria., No structural information is so far available for the 3' incision, reaction. Here we report the crystal structure of the N-terminal catalytic, domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision, reaction and shares homology with the catalytic domain of the GIY-YIG, family of intron-encoded homing endonucleases. The structure reveals a, patch of highly conserved residues surrounding a catalytic magnesium-water, cluster, suggesting that the metal binding site is an essential feature of, UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data, strongly suggest that the N-terminal endonuclease domain of UvrC utilizes, a novel one-metal mechanism to cleave the phosphodiester bond.

Nucleotide excision repair is a highly conserved DNA repair mechanism present in all kingdoms of life. The incision reaction is a critical step for damage removal and is accomplished by the UvrC protein in eubacteria. No structural information is so far available for the 3' incision reaction. Here we report the crystal structure of the N-terminal catalytic domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision reaction and shares homology with the catalytic domain of the GIY-YIG family of intron-encoded homing endonucleases. The structure reveals a patch of highly conserved residues surrounding a catalytic magnesium-water cluster, suggesting that the metal binding site is an essential feature of UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data strongly suggest that the N-terminal endonuclease domain of UvrC utilizes a novel one-metal mechanism to cleave the phosphodiester bond.

==About this Structure==

1YD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1YD4 OCA].

1YD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] 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=1YD4 OCA].

==Reference==

Line 13:

[[Category: Single protein]]

[[Category: Thermotoga maritima]]

[[Category: Croteau, D.L.]]

[[Category: Croteau, D L.]]

[[Category: DellaVecchia, M.J.]]

[[Category: DellaVecchia, M J.]]

[[Category: Houten, B.Van.]]

[[Category: Houten, B Van.]]

[[Category: Karakas, E.]]

[[Category: Kisker, C.]]

[[Category: Rhau, B.]]

[[Category: Skorvaga, M.]]

[[Category: Truglio, J.J.]]

[[Category: Truglio, J J.]]

[[Category: Wang, H.]]

[[Category: Wang, L.]]

Line 26:

[[Category: dna binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 06:41:~~40 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:05 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1yd4.gif|left|200px]]<br /><applet load="1yd4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1yd4.gif|left|200px]]<br /><applet load="1yd4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1yd4, resolution 1.90&Aring;" />
 '''Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y29F bound to its catalytic divalent cation'''<br />
 ==Overview==
-Nucleotide excision repair is a highly conserved DNA repair mechanism, present in all kingdoms of life. The incision reaction is a critical step, for damage removal and is accomplished by the UvrC protein in eubacteria., No structural information is so far available for the 3' incision, reaction. Here we report the crystal structure of the N-terminal catalytic, domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision, reaction and shares homology with the catalytic domain of the GIY-YIG, family of intron-encoded homing endonucleases. The structure reveals a, patch of highly conserved residues surrounding a catalytic magnesium-water, cluster, suggesting that the metal binding site is an essential feature of, UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data, strongly suggest that the N-terminal endonuclease domain of UvrC utilizes, a novel one-metal mechanism to cleave the phosphodiester bond.
+Nucleotide excision repair is a highly conserved DNA repair mechanism present in all kingdoms of life. The incision reaction is a critical step for damage removal and is accomplished by the UvrC protein in eubacteria. No structural information is so far available for the 3' incision reaction. Here we report the crystal structure of the N-terminal catalytic domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision reaction and shares homology with the catalytic domain of the GIY-YIG family of intron-encoded homing endonucleases. The structure reveals a patch of highly conserved residues surrounding a catalytic magnesium-water cluster, suggesting that the metal binding site is an essential feature of UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data strongly suggest that the N-terminal endonuclease domain of UvrC utilizes a novel one-metal mechanism to cleave the phosphodiester bond.
 ==About this Structure==
-YD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YD4 OCA].
+YD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] 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=1YD4 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Croteau, D.L.]]
+[[Category: Croteau, D L.]]
-[[Category: DellaVecchia, M.J.]]
+[[Category: DellaVecchia, M J.]]
-[[Category: Houten, B.Van.]]
+[[Category: Houten, B Van.]]
 [[Category: Karakas, E.]]
 [[Category: Kisker, C.]]
 [[Category: Rhau, B.]]
 [[Category: Skorvaga, M.]]
-[[Category: Truglio, J.J.]]
+[[Category: Truglio, J J.]]
 [[Category: Wang, H.]]
 [[Category: Wang, L.]]
@@ Line 26: / Line 26: @@
 [[Category: dna binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:41:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:05 2008''