1v92: Difference between revisions

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[[Image:1v92.gif|left|200px]]<br /><applet load="1v92" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1v92.gif|left|200px]]<br /><applet load="1v92" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1v92" />

'''Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97'''<br />

==Overview==

p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The, principal role of the p97-p47 complex is in regulation of membrane fusion, events. Mono-ubiquitin recognition by p47 has also been shown to be, crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we, describe the high-resolution solution structures of the N-terminal UBA, domain and the central domain (SEP) from p47. The p47 UBA domain has the, characteristic three-helix bundle fold and forms a highly stable complex, with ubiquitin. We report the interaction surfaces of the two proteins and, present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain, adopts a novel fold with a betabetabetaalphaalphabeta secondary structure, arrangement, where beta4 pairs in a parallel fashion to beta1. Based on, biophysical studies, we demonstrate a clear propensity for the, self-association of p47. Furthermore, p97 N binding abolishes p47, self-association, revealing the potential interaction surfaces for, recognition of other domains within p97 or the substrate.

p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The principal role of the p97-p47 complex is in regulation of membrane fusion events. Mono-ubiquitin recognition by p47 has also been shown to be crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we describe the high-resolution solution structures of the N-terminal UBA domain and the central domain (SEP) from p47. The p47 UBA domain has the characteristic three-helix bundle fold and forms a highly stable complex with ubiquitin. We report the interaction surfaces of the two proteins and present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain adopts a novel fold with a betabetabetaalphaalphabeta secondary structure arrangement, where beta4 pairs in a parallel fashion to beta1. Based on biophysical studies, we demonstrate a clear propensity for the self-association of p47. Furthermore, p97 N binding abolishes p47 self-association, revealing the potential interaction surfaces for recognition of other domains within p97 or the substrate.

==About this Structure==

1V92 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1V92 OCA].

1V92 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V92 OCA].

==Reference==

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[[Category: 3-helix bundle]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:46 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1v92.gif|left|200px]]<br /><applet load="1v92" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1v92.gif|left|200px]]<br /><applet load="1v92" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1v92" />
 '''Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97'''<br />
 ==Overview==
-p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The, principal role of the p97-p47 complex is in regulation of membrane fusion, events. Mono-ubiquitin recognition by p47 has also been shown to be, crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we, describe the high-resolution solution structures of the N-terminal UBA, domain and the central domain (SEP) from p47. The p47 UBA domain has the, characteristic three-helix bundle fold and forms a highly stable complex, with ubiquitin. We report the interaction surfaces of the two proteins and, present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain, adopts a novel fold with a betabetabetaalphaalphabeta secondary structure, arrangement, where beta4 pairs in a parallel fashion to beta1. Based on, biophysical studies, we demonstrate a clear propensity for the, self-association of p47. Furthermore, p97 N binding abolishes p47, self-association, revealing the potential interaction surfaces for, recognition of other domains within p97 or the substrate.
+p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The principal role of the p97-p47 complex is in regulation of membrane fusion events. Mono-ubiquitin recognition by p47 has also been shown to be crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we describe the high-resolution solution structures of the N-terminal UBA domain and the central domain (SEP) from p47. The p47 UBA domain has the characteristic three-helix bundle fold and forms a highly stable complex with ubiquitin. We report the interaction surfaces of the two proteins and present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain adopts a novel fold with a betabetabetaalphaalphabeta secondary structure arrangement, where beta4 pairs in a parallel fashion to beta1. Based on biophysical studies, we demonstrate a clear propensity for the self-association of p47. Furthermore, p97 N binding abolishes p47 self-association, revealing the potential interaction surfaces for recognition of other domains within p97 or the substrate.
 ==About this Structure==
-V92 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V92 OCA].
+V92 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V92 OCA].
 ==Reference==
@@ Line 27: / Line 27: @@
 [[Category: 3-helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:31:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:46 2008''