1e32: Difference between revisions

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New page: left|200px<br /><applet load="1e32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e32, resolution 2.9Å" /> '''STRUCTURE OF THE N-TE...
 
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[[Image:1e32.gif|left|200px]]<br /><applet load="1e32" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1e32.gif|left|200px]]<br /><applet load="1e32" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1e32, resolution 2.9&Aring;" />
caption="1e32, resolution 2.9&Aring;" />
'''STRUCTURE OF THE N-TERMINAL DOMAIN AND THE D1 AAA DOMAIN OF MEMBRANE FUSION ATPASE P97'''<br />
'''STRUCTURE OF THE N-TERMINAL DOMAIN AND THE D1 AAA DOMAIN OF MEMBRANE FUSION ATPASE P97'''<br />


==Overview==
==Overview==
p97, an abundant hexameric ATPase of the AAA family, is involved in, homotypic membrane fusion. It is thought to disassemble SNARE complexes, formed during the process of membrane fusion. Here, we report two, structures: a crystal structure of the N-terminal and D1 ATPase domains of, murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure of, full-length rat p97 at 18 A resolution. Together, these structures show, that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and that, the N domain is flexible. A comparison with NSF D2 (ATP complex) reveals, possible conformational changes induced by ATP hydrolysis. Given the D1, and D2 packing arrangement, we propose a ratchet mechanism for p97 during, its ATP hydrolysis cycle.
p97, an abundant hexameric ATPase of the AAA family, is involved in homotypic membrane fusion. It is thought to disassemble SNARE complexes formed during the process of membrane fusion. Here, we report two structures: a crystal structure of the N-terminal and D1 ATPase domains of murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 A resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and that the N domain is flexible. A comparison with NSF D2 (ATP complex) reveals possible conformational changes induced by ATP hydrolysis. Given the D1 and D2 packing arrangement, we propose a ratchet mechanism for p97 during its ATP hydrolysis cycle.


==About this Structure==
==About this Structure==
1E32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E32 OCA].  
1E32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E32 OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bates, P.A.]]
[[Category: Bates, P A.]]
[[Category: Dokurno, P.]]
[[Category: Dokurno, P.]]
[[Category: Freemont, P.S.]]
[[Category: Freemont, P S.]]
[[Category: Gorman, M.A.]]
[[Category: Gorman, M A.]]
[[Category: Kondo, H.]]
[[Category: Kondo, H.]]
[[Category: Shaw, A.]]
[[Category: Shaw, A.]]
[[Category: Sternberg, G.Leon M.J.E.]]
[[Category: Sternberg, G Leon M J.E.]]
[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
[[Category: ADP]]
[[Category: ADP]]
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[[Category: membrane fusion]]
[[Category: membrane fusion]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:45:23 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:17 2008''

Revision as of 13:23, 21 February 2008

File:1e32.gif


1e32, resolution 2.9Å

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STRUCTURE OF THE N-TERMINAL DOMAIN AND THE D1 AAA DOMAIN OF MEMBRANE FUSION ATPASE P97

OverviewOverview

p97, an abundant hexameric ATPase of the AAA family, is involved in homotypic membrane fusion. It is thought to disassemble SNARE complexes formed during the process of membrane fusion. Here, we report two structures: a crystal structure of the N-terminal and D1 ATPase domains of murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 A resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and that the N domain is flexible. A comparison with NSF D2 (ATP complex) reveals possible conformational changes induced by ATP hydrolysis. Given the D1 and D2 packing arrangement, we propose a ratchet mechanism for p97 during its ATP hydrolysis cycle.

About this StructureAbout this Structure

1E32 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the AAA ATPase p97., Zhang X, Shaw A, Bates PA, Newman RH, Gowen B, Orlova E, Gorman MA, Kondo H, Dokurno P, Lally J, Leonard G, Meyer H, van Heel M, Freemont PS, Mol Cell. 2000 Dec;6(6):1473-84. PMID:11163219

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