1i42: Difference between revisions

Line 1:

[[Image:1i42.gif|left|200px]]<br /><applet load="1i42" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1i42.gif|left|200px]]<br /><applet load="1i42" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1i42" />

'''NMR STRUCTURE OF THE UBX DOMAIN FROM P47'''<br />

==Overview==

p47 is the major protein identified in complex with the cytosolic AAA, ATPase p97. It functions as an essential cofactor of p97-regulated, membrane fusion, which has been suggested to disassemble t-t-SNARE, complexes and prepare them for further rounds of membrane fusion. Here, we, report the high-resolution NMR structure of the C-terminal domain from, p47. It comprises a UBX domain and a 13 residue long structured N-terminal, extension. The UBX domain adopts a characteristic ubiquitin fold with a, betabetaalphabetabetaalphabeta secondary structure arrangement. Three, hydrophobic residues from the N-terminal extension pack closely against a, cleft in the UBX domain. We also identify, for the first time, the p97, interaction surface using NMR chemical shift perturbation studies.

p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a betabetaalphabetabetaalphabeta secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies.

==About this Structure==

1I42 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=1I42 OCA].

1I42 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=1I42 OCA].

==Reference==

Line 13:

[[Category: Rattus norvegicus]]

[[Category: Single protein]]

[[Category: Freemont, P.S.]]

[[Category: Freemont, P S.]]

[[Category: Kondo, H.]]

[[Category: Lally, J.]]

Line 24:

[[Category: unusual n-terminal feature]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:02:~~22 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:45 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1i42.gif|left|200px]]<br /><applet load="1i42" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1i42.gif|left|200px]]<br /><applet load="1i42" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1i42" />
 '''NMR STRUCTURE OF THE UBX DOMAIN FROM P47'''<br />
 ==Overview==
-p47 is the major protein identified in complex with the cytosolic AAA, ATPase p97. It functions as an essential cofactor of p97-regulated, membrane fusion, which has been suggested to disassemble t-t-SNARE, complexes and prepare them for further rounds of membrane fusion. Here, we, report the high-resolution NMR structure of the C-terminal domain from, p47. It comprises a UBX domain and a 13 residue long structured N-terminal, extension. The UBX domain adopts a characteristic ubiquitin fold with a, betabetaalphabetabetaalphabeta secondary structure arrangement. Three, hydrophobic residues from the N-terminal extension pack closely against a, cleft in the UBX domain. We also identify, for the first time, the p97, interaction surface using NMR chemical shift perturbation studies.
+p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a betabetaalphabetabetaalphabeta secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies.
 ==About this Structure==
-I42 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=1I42 OCA].
+I42 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=1I42 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Freemont, P.S.]]
+[[Category: Freemont, P S.]]
 [[Category: Kondo, H.]]
 [[Category: Lally, J.]]
@@ Line 24: / Line 24: @@
 [[Category: unusual n-terminal feature]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:02:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:45 2008''