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New page: left|200px<br /><applet load="1euv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1euv, resolution 1.6Å" /> '''X-RAY STRUCTURE OF TH...
 
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[[Image:1euv.gif|left|200px]]<br /><applet load="1euv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1euv.gif|left|200px]]<br /><applet load="1euv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1euv, resolution 1.6&Aring;" />
caption="1euv, resolution 1.6&Aring;" />
'''X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.'''<br />
'''X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.'''<br />


==Overview==
==Overview==
Modification of cellular proteins by the ubiquitin-like protein SUMO is, essential for nuclear processes and cell cycle progression in yeast. The, Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1), processing of full-length SUMO to its mature form and (2) deconjugation of, SUMO from targeted proteins. Selective reduction of the proteolytic, reaction produced a covalent thiohemiacetal transition state complex, between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the, yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing, of elements within the conserved interface elucidate determinants of SUMO, recognition, processing, and deconjugation. Genetic analysis guided by the, structure further reveals a regulatory element N-terminal to the, proteolytic domain that is required for cell growth in yeast.
Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear processes and cell cycle progression in yeast. The Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1) processing of full-length SUMO to its mature form and (2) deconjugation of SUMO from targeted proteins. Selective reduction of the proteolytic reaction produced a covalent thiohemiacetal transition state complex between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing of elements within the conserved interface elucidate determinants of SUMO recognition, processing, and deconjugation. Genetic analysis guided by the structure further reveals a regulatory element N-terminal to the proteolytic domain that is required for cell growth in yeast.


==About this Structure==
==About this Structure==
1EUV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EUV OCA].  
1EUV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUV OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Lima, C.D.]]
[[Category: Lima, C D.]]
[[Category: Mossessova, E.]]
[[Category: Mossessova, E.]]
[[Category: covalent protease adduct]]
[[Category: covalent protease adduct]]
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[[Category: ubiquitin-like protease 1]]
[[Category: ubiquitin-like protease 1]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:20:06 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:43 2008''