1n87: Difference between revisions

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New page: left|200px<br /><applet load="1n87" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n87" /> '''Solution structure of the U-box of Prp19'''<...
 
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[[Image:1n87.gif|left|200px]]<br /><applet load="1n87" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1n87.gif|left|200px]]<br /><applet load="1n87" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1n87" />
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'''Solution structure of the U-box of Prp19'''<br />
'''Solution structure of the U-box of Prp19'''<br />


==Overview==
==Overview==
The structure of the U-box in the essential Saccharomyces cerevisiae, pre-mRNA splicing factor Prp19p has been determined by NMR. The conserved, zinc-binding sites supporting the cross-brace arrangement in RING-finger, domains are replaced by hydrogen-bonding networks in the U-box. These, hydrogen-bonding networks are necessary for the structural stabilization, and activity of the U-box. A conservative Val--&gt;Ile point mutation in the, Prp19p U-box domain leads to pre-mRNA splicing defects in vivo. NMR, analysis of this mutant shows that the substitution disrupts structural, integrity of the U-box domain. Furthermore, comparison of the Prp19p U-box, domain with known RING-E2 complex structures demonstrates that both U-box, and RING-fingers contain a conserved interaction surface. Mutagenesis of, residues at this interface, while not perturbing the structure of the, U-box, abrogates Prp19p function in vivo. These comparative structural and, functional analyses imply that the U-box and its associated ubiquitin, ligase activity are critical for Prp19p function in vivo.
The structure of the U-box in the essential Saccharomyces cerevisiae pre-mRNA splicing factor Prp19p has been determined by NMR. The conserved zinc-binding sites supporting the cross-brace arrangement in RING-finger domains are replaced by hydrogen-bonding networks in the U-box. These hydrogen-bonding networks are necessary for the structural stabilization and activity of the U-box. A conservative Val--&gt;Ile point mutation in the Prp19p U-box domain leads to pre-mRNA splicing defects in vivo. NMR analysis of this mutant shows that the substitution disrupts structural integrity of the U-box domain. Furthermore, comparison of the Prp19p U-box domain with known RING-E2 complex structures demonstrates that both U-box and RING-fingers contain a conserved interaction surface. Mutagenesis of residues at this interface, while not perturbing the structure of the U-box, abrogates Prp19p function in vivo. These comparative structural and functional analyses imply that the U-box and its associated ubiquitin ligase activity are critical for Prp19p function in vivo.


==About this Structure==
==About this Structure==
1N87 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1N87 OCA].  
1N87 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1N87 OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chazin, W.J.]]
[[Category: Chazin, W J.]]
[[Category: Kooi, C.W.Vander.]]
[[Category: Kooi, C W.Vander.]]
[[Category: Ohi, M.D.]]
[[Category: Ohi, M D.]]
[[Category: e3 ligase]]
[[Category: e3 ligase]]
[[Category: u-box]]
[[Category: u-box]]
[[Category: ubiquitin ligase]]
[[Category: ubiquitin ligase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:22 2008''

Revision as of 15:03, 21 February 2008

File:1n87.gif


1n87

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Solution structure of the U-box of Prp19

OverviewOverview

The structure of the U-box in the essential Saccharomyces cerevisiae pre-mRNA splicing factor Prp19p has been determined by NMR. The conserved zinc-binding sites supporting the cross-brace arrangement in RING-finger domains are replaced by hydrogen-bonding networks in the U-box. These hydrogen-bonding networks are necessary for the structural stabilization and activity of the U-box. A conservative Val-->Ile point mutation in the Prp19p U-box domain leads to pre-mRNA splicing defects in vivo. NMR analysis of this mutant shows that the substitution disrupts structural integrity of the U-box domain. Furthermore, comparison of the Prp19p U-box domain with known RING-E2 complex structures demonstrates that both U-box and RING-fingers contain a conserved interaction surface. Mutagenesis of residues at this interface, while not perturbing the structure of the U-box, abrogates Prp19p function in vivo. These comparative structural and functional analyses imply that the U-box and its associated ubiquitin ligase activity are critical for Prp19p function in vivo.

About this StructureAbout this Structure

1N87 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structural insights into the U-box, a domain associated with multi-ubiquitination., Ohi MD, Vander Kooi CW, Rosenberg JA, Chazin WJ, Gould KL, Nat Struct Biol. 2003 Apr;10(4):250-5. PMID:12627222

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