We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1i42

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1i42" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i42" /> '''NMR STRUCTURE OF THE UBX DOMAIN FROM P47'''<...)
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" />
caption="1i42" />
'''NMR STRUCTURE OF THE UBX DOMAIN FROM P47'''<br />
'''NMR STRUCTURE OF THE UBX DOMAIN FROM P47'''<br />
==Overview==
==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==
==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==
==Reference==
Line 13: Line 13:
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Freemont, P.S.]]
+
[[Category: Freemont, P S.]]
[[Category: Kondo, H.]]
[[Category: Kondo, H.]]
[[Category: Lally, J.]]
[[Category: Lally, J.]]
Line 24: Line 24:
[[Category: unusual n-terminal feature]]
[[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''

Revision as of 11:07, 21 February 2008


1i42

Drag the structure with the mouse to rotate

NMR STRUCTURE OF THE UBX DOMAIN FROM P47

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.

About this Structure

1I42 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly., Yuan X, Shaw A, Zhang X, Kondo H, Lally J, Freemont PS, Matthews S, J Mol Biol. 2001 Aug 10;311(2):255-63. PMID:11478859

Page seeded by OCA on Thu Feb 21 13:07:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools