2qpa
From Proteopedia
(New page: 200px<br /><applet load="2qpa" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qpa, resolution 3.200Å" /> '''Crystal Structure o...) |
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caption="2qpa, resolution 3.200Å" /> | caption="2qpa, resolution 3.200Å" /> | ||
'''Crystal Structure of S.cerevisiae Vps4 in the presence of ADP'''<br /> | '''Crystal Structure of S.cerevisiae Vps4 in the presence of ADP'''<br /> | ||
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| + | ==Overview== | ||
| + | The multivesicular body (MVB) pathway functions in multiple cellular, processes including cell surface receptor down-regulation and viral, budding from host cells. An important step in the MVB pathway is the, correct sorting of cargo molecules, which requires the assembly and, disassembly of endosomal sorting complexes required for transport (ESCRTs), on the endosomal membrane. Disassembly of the ESCRTs is catalyzed by, ATPase associated with various cellular activities (AAA) protein Vps4., Vps4 contains a single AAA domain and undergoes ATP-dependent quaternary, structural change to disassemble the ESCRTs. Structural and biochemical, analyses of the Vps4 ATPase reaction cycle are reported here. Crystal, structures of Saccharomyces cerevisiae Vps4 in both the nucleotide-free, form and the ADP-bound form provide the first structural view illustrating, how nucleotide binding might induce conformational changes within Vps4, that lead to oligomerization and binding to its substrate ESCRT-III, subunits. In contrast to previous models, characterization of the Vps4, structure now supports a model where the ground state of Vps4 in the, ATPase reaction cycle is predominantly a monomer and the activated state, is a dodecamer. Comparison with a previously reported human VPS4B, structure suggests that Vps4 functions in the MVB pathway via a highly, conserved mechanism supported by similar protein-protein interactions, during its ATPase reaction cycle. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2QPA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPA OCA]. | + | 2QPA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Po4 Binding Site For Residue B 800'>AC1</scene>, <scene name='pdbsite=AC2:Po4 Binding Site For Residue C 800'>AC2</scene> and <scene name='pdbsite=AC3:Adp Binding Site For Residue A 800'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPA OCA]. |
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| + | ==Reference== | ||
| + | Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4., Xiao J, Xia H, Yoshino-Koh K, Zhou J, Xu Z, J Mol Biol. 2007 Nov 30;374(3):655-70. Epub 2007 Sep 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17949747 17949747] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: vacuole]] | [[Category: vacuole]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:59:22 2008'' |
Revision as of 08:59, 31 January 2008
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Crystal Structure of S.cerevisiae Vps4 in the presence of ADP
Overview
The multivesicular body (MVB) pathway functions in multiple cellular, processes including cell surface receptor down-regulation and viral, budding from host cells. An important step in the MVB pathway is the, correct sorting of cargo molecules, which requires the assembly and, disassembly of endosomal sorting complexes required for transport (ESCRTs), on the endosomal membrane. Disassembly of the ESCRTs is catalyzed by, ATPase associated with various cellular activities (AAA) protein Vps4., Vps4 contains a single AAA domain and undergoes ATP-dependent quaternary, structural change to disassemble the ESCRTs. Structural and biochemical, analyses of the Vps4 ATPase reaction cycle are reported here. Crystal, structures of Saccharomyces cerevisiae Vps4 in both the nucleotide-free, form and the ADP-bound form provide the first structural view illustrating, how nucleotide binding might induce conformational changes within Vps4, that lead to oligomerization and binding to its substrate ESCRT-III, subunits. In contrast to previous models, characterization of the Vps4, structure now supports a model where the ground state of Vps4 in the, ATPase reaction cycle is predominantly a monomer and the activated state, is a dodecamer. Comparison with a previously reported human VPS4B, structure suggests that Vps4 functions in the MVB pathway via a highly, conserved mechanism supported by similar protein-protein interactions, during its ATPase reaction cycle.
About this Structure
2QPA is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4., Xiao J, Xia H, Yoshino-Koh K, Zhou J, Xu Z, J Mol Biol. 2007 Nov 30;374(3):655-70. Epub 2007 Sep 29. PMID:17949747
Page seeded by OCA on Thu Jan 31 10:59:22 2008
Categories: Saccharomyces cerevisiae | Single protein | Xiao, J. | Xu, Z. | ADP | PO4 | Adp | Atp-binding | Atpase domain | Beta domain | C-terminal helix | Endosome | Nucleotide-binding | Protein transport | Proton transport | Transport | Vacuole
