2io2: Difference between revisions

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[[Image:2io2.gif|left|200px]]<br />

[[Image:2io2.gif|left|200px]]<br /><applet load="2io2" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2io2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2io2, resolution 2.900Å" />

'''Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1'''<br />

==Overview==

SUMO processing and deconjugation are essential proteolytic activities for, nuclear metabolism and cell-cycle progression in yeast and higher, eukaryotes. To elucidate the mechanisms used during substrate lysine, deconjugation, SUMO isoform processing and SUMO isoform interactions, X-ray structures were determined for a catalytically inert SENP2 protease, domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in, complex with SUMO-2 or SUMO-3 precursors. Common features within the, active site include a 90 degrees kink proximal to the scissile bond that, forces C-terminal amino acid residues or the lysine side chain toward a, protease surface that appears optimized for lysine deconjugation. Analysis, of this surface reveals SENP2 residues, particularly Met497, that mediate, and in some instances reverse, in vitro substrate specificity. Mutational, analysis and biochemistry provide a mechanism for SENP2 substrate, preferences that explains why SENP2 catalyzes SUMO deconjugation more, efficiently than processing.

SUMO processing and deconjugation are essential proteolytic activities for nuclear metabolism and cell-cycle progression in yeast and higher eukaryotes. To elucidate the mechanisms used during substrate lysine deconjugation, SUMO isoform processing and SUMO isoform interactions, X-ray structures were determined for a catalytically inert SENP2 protease domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in complex with SUMO-2 or SUMO-3 precursors. Common features within the active site include a 90 degrees kink proximal to the scissile bond that forces C-terminal amino acid residues or the lysine side chain toward a protease surface that appears optimized for lysine deconjugation. Analysis of this surface reveals SENP2 residues, particularly Met497, that mediate, and in some instances reverse, in vitro substrate specificity. Mutational analysis and biochemistry provide a mechanism for SENP2 substrate preferences that explains why SENP2 catalyzes SUMO deconjugation more efficiently than processing.

==Disease==

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==About this Structure==

2IO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2IO2 OCA].

2IO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IO2 OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Lima, C.D.]]

[[Category: Lima, C D.]]

[[Category: Reverter, D.]]

[[Category: complex]]

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[[Category: ulp]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:46:~~25 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:27 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2io2.gif|left|200px]]<br />
+[[Image:2io2.gif|left|200px]]<br /><applet load="2io2" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2io2" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2io2, resolution 2.900&Aring;" />
 '''Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1'''<br />
 ==Overview==
-SUMO processing and deconjugation are essential proteolytic activities for, nuclear metabolism and cell-cycle progression in yeast and higher, eukaryotes. To elucidate the mechanisms used during substrate lysine, deconjugation, SUMO isoform processing and SUMO isoform interactions, X-ray structures were determined for a catalytically inert SENP2 protease, domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in, complex with SUMO-2 or SUMO-3 precursors. Common features within the, active site include a 90 degrees kink proximal to the scissile bond that, forces C-terminal amino acid residues or the lysine side chain toward a, protease surface that appears optimized for lysine deconjugation. Analysis, of this surface reveals SENP2 residues, particularly Met497, that mediate, and in some instances reverse, in vitro substrate specificity. Mutational, analysis and biochemistry provide a mechanism for SENP2 substrate, preferences that explains why SENP2 catalyzes SUMO deconjugation more, efficiently than processing.
+SUMO processing and deconjugation are essential proteolytic activities for nuclear metabolism and cell-cycle progression in yeast and higher eukaryotes. To elucidate the mechanisms used during substrate lysine deconjugation, SUMO isoform processing and SUMO isoform interactions, X-ray structures were determined for a catalytically inert SENP2 protease domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in complex with SUMO-2 or SUMO-3 precursors. Common features within the active site include a 90 degrees kink proximal to the scissile bond that forces C-terminal amino acid residues or the lysine side chain toward a protease surface that appears optimized for lysine deconjugation. Analysis of this surface reveals SENP2 residues, particularly Met497, that mediate, and in some instances reverse, in vitro substrate specificity. Mutational analysis and biochemistry provide a mechanism for SENP2 substrate preferences that explains why SENP2 catalyzes SUMO deconjugation more efficiently than processing.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-IO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IO2 OCA].
+IO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IO2 OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Lima, C.D.]]
+[[Category: Lima, C D.]]
 [[Category: Reverter, D.]]
 [[Category: complex]]
@@ Line 25: / Line 24: @@
 [[Category: ulp]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:46:25 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:27 2008''