2io0: Difference between revisions

Revision as of 18:54, 21 February 2008

Crystal structure of human Senp2 in complex with preSUMO-2

OverviewOverview

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.

About this StructureAbout this Structure

2IO0 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates., Reverter D, Lima CD, Nat Struct Mol Biol. 2006 Dec;13(12):1060-8. Epub 2006 Nov 12. PMID:17099700

Page seeded by OCA on Thu Feb 21 17:54:27 2008

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OCA

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-[[Image:2io0.gif|left|200px]]<br />
+[[Image:2io0.gif|left|200px]]<br /><applet load="2io0" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2io0" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2io0, resolution 2.300&Aring;" />
 '''Crystal structure of human Senp2 in complex with preSUMO-2'''<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.
 ==About this Structure==
-IO0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IO0 OCA].
+IO0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IO0 OCA].
 ==Reference==
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 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Lima, C.D.]]
+[[Category: Lima, C D.]]
 [[Category: Reverter, D.]]
 [[Category: SO4]]
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 [[Category: ulp]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:46:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:27 2008''